Cshperspect-REP-A015727 Table3 1..10

Total Page:16

File Type:pdf, Size:1020Kb

Cshperspect-REP-A015727 Table3 1..10 Table 3. Nomenclature for proteins and protein complexes in different organisms Mammals Budding yeast Fission yeast Flies Plants Archaea Bacteria Prereplication complex assembly H. sapiens S. cerevisiae S. pombe D. melanogaster A. thaliana S. solfataricus E. coli Hs Sc Sp Dm At Sso Eco ORC ORC ORC ORC ORC [Orc1/Cdc6]-1, 2, 3 DnaA Orc1/p97 Orc1/p104 Orc1/Orp1/p81 Orc1/p103 Orc1a, Orc1b Orc2/p82 Orc2/p71 Orc2/Orp2/p61 Orc2/p69 Orc2 Orc3/p66 Orc3/p72 Orc3/Orp3/p80 Orc3/Lat/p82 Orc3 Orc4/p50 Orc4/p61 Orc4/Orp4/p109 Orc4/p52 Orc4 Orc5L/p50 Orc5/p55 Orc5/Orp5/p52 Orc5/p52 Orc5 Orc6/p28 Orc6/p50 Orc6/Orp6/p31 Orc6/p29 Orc6 Cdc6 Cdc6 Cdc18 Cdc6 Cdc6a, Cdc6b [Orc1/Cdc6]-1, 2, 3 DnaC Cdt1/Rlf-B Tah11/Sid2/Cdt1 Cdt1 Dup/Cdt1 Cdt1a, Cdt1b Whip g MCM helicase MCM helicase MCM helicase MCM helicase MCM helicase Mcm DnaB Mcm2 Mcm2 Mcm2/Nda1/Cdc19 Mcm2 Mcm2 Mcm3 Mcm3 Mcm3 Mcm3 Mcm3 Mcm4 Mcm4/Cdc54 Mcm4/Cdc21 Mcm4/Dpa Mcm4 Mcm5 Mcm5/Cdc46/Bob1 Mcm5/Nda4 Mcm5 Mcm5 Mcm6 Mcm6 Mcm6/Mis5 Mcm6 Mcm6 Mcm7 Mcm7/Cdc47 Mcm7 Mcm7 Mcm7/Prolifera Gmnn/Geminin Geminin Mcm9 Mcm9 Hbo1 Chm/Hat1 Ham1 Ham2 DiaA Ihfa Ihfb Fis SeqA Replication fork assembly Hs Sc Sp Dm At Sso Eco Mcm8 Rec/Mcm8 Mcm8 Mcm10 Mcm10/Dna43 Mcm10/Cdc23 Mcm10 Mcm10 DDK complex DDK complex DDK complex DDK complex Cdc7 Cdc7 Hsk1 l(1)G0148 Hsk1-like 1 Dbf4/Ask Dbf4 Dfp1/Him1/Rad35 Chif/chiffon Drf1 Continued 2 Replication fork assembly (Continued ) Hs Sc Sp Dm At Sso Eco CDK complex CDK complex CDK complex CDK complex CDK complex Cdk1 Cdc28/Cdk1 Cdc2/Cdk1 Cdc2 CdkA Cdk2 Cdc2c CcnA1, A2 CycA CycA1, A2, A3 CcnB1, B2, B3 Clb1 to Clb6 Cig2/Cyc17, Cig1, Cdc13 CycB, B3 CycB1, B2, B3 CcnE1, E2 CycE Cdc45 Cdc45 Cdc45/Sna41/Goa1 Cdc45 Cdc45 PP2A PP2A PP2A PP2A PP2A RecQL4 Sld2/Drc1 Drc1 RecQL4 Treslin Sld3 Sld3 Sld3 TopBP1 Dpb11 Rad4/Cut5 Mus101 Topbp1 GINS complex GINS complex GINS complex GINS complex GINS complex Gins4 Sld5/Cdc105 Sld5 Sld5 Sld5 Gins 23 Gins1 Psf1/Cdc101 Psf1 Psf1 Psf1 Gins 15 Gins2 Psf2/Cdc102 Psf2 Psf2 Psf2 Gins3 Psf3/Cdc103 Psf3 Psf3 Psf3a, Psf3b DNA synthesis at replication forks Hs Sc Sp Dm At Sso Eco DNA Pol a DNA Pol a DNA Pol a DNA Pol a DNA Pol a DNA Pol B DNA Pol III core PolA/p180 Pol1/Cdc17/Crt5/Lrs9/Hpr3 Pol1 DNA Pol a180 Pola1 enzyme PolA2/p68 Pol12 Spb70/Pol12 DNA Pol a60 Pola2 DNA primase DNA primase DNA primase DNA primase DNA primase DNA primase DnaG Prim1/p48 Pri1 Spp1 DNA Pol a50 Pola3/Pri1 PriS/p38 Prim2a/p58 Pri2 Spp2 DNA Pol a73 Pola4/Pri2 PriL/p36 DNA Pol d DNA Pol d DNA Pol d DNA Pol d DNA Pol d DNA Pol Db DNA Pol III Pold1/p125 Cdc2/Pol3/Hpr6/Tex 1 Cdc6/Pol3/Mis10 DNA Pol d138 Pold1 holoenzyme Pold2/p50 Hys2/Pol31/Hus2/Sdp5 Cdc1/Mis1 DNA Pol d47 Pold2 Pold3/p66 Pol32 Cdc27 Pold3 Pold4/p12 Cdm1 Pold4 DNA Pol 1 DNA Pol 1 DNA Pol 1 DNA Pol 1 DNA Pol 1 DNA Pol B DNA Pol III Pole/p261 Pol2/Dun2 Cdc20/Pol2 DNA Pol 1 Pole1a, Pole1b holoenzyme Pole2/p59 Dpb2 Dpb2 Pole2 Pole3/p17 Dpb3 Dpb3 Pole3 Pole4/p12 Dpb4 Dpb4 Pole4 DNA Pol g DNA Pol g DNA Pol g DNA Pol g Polg/p140 Mip1 Mip1 Tam/Tamas/-g125 Polg2/p55 DNA Pol g35 RPA complex RPA complex RPA complex RPA complex RPA complex SSB SSB Rpa1/p70 Rfa1/Buf2/Fun3/Rpa1 Ssb1/Rad11/Rpa1 Rpa70 Rpa1a, Rpa1b Rpa1c, Rpa1d Rpa2/p32 Rfa2/Buf1/Rpa2 Ssb2 Rpa30 Rpa2a, Rpa2b Rpa3/p14 Rfa3 Ssb3/Rpa3 Rpa8 Rpa3a, Rpa3b PCNA Pol30 Pcn1 Mus209 PCNA1 PCNA1 b-clamp PCNA2 PCNA2 PCNA3 RFC clamp loader RFC clamp loader RFC clamp loader RFC clamp loader RFC clamp loader RFC clamp loader Fork clamp loader RNaseH2 complex RNaseH2 complex Rnaseh2a Rnh201/Rnh35 Rnh201 Rnh 1 RnaseH2 RnaseH2 RNaseH Rnaseh2b Rnh202 Rnaseh2c Rnh203 Dna2 Dna2/Web2 Dna2 CG2990 Dna2 DNA Pol I Fen1 Rad27/Erc11/Rth1 Rad2/Fen1 Fen1 Fen1 Fen1 DNA Pol I Lig1 Cdc9/Mms8 Cdc17 DNA-ligI Lig1a, Lig1b Lig1 Lig Top1/Topo I Top1/Mak1/Mak17 Top1 Top1 Top1a, Top1b Topo I,c Topo III DNA gyrase Top2/Topo II Top2/Tor3/Trf3 Top2/Ptr11 Top2 Top2 DNA gyrasec DNA gyrase Topo VI Topo IV CDK inhibitors Cdkn1a/p21/Cip1 Cdkn1b/p27/Kip1 Sic1/p40/Sdb25a Rum1/p25a Dap/Dacapo/p26 Krp1 to Krp7 Cdkn1c/p57/Kip2 Replication fork progression and stability Hs Sc Sp Dm At Sso Eco Clspn/Claspin Mrc1 Mrc1/Huc1 Timeless Tof1 Swi1 Tim/Timeless Tim1 Tipin Csm3 Swi3 Elg1-RFC clamp loader Elg1-RFC clamp loader Elg1-RFC clamp loader Brca2/FANCd1 Brca2a, Brca2b Continued 3 4 Replication fork progression and stability (Continued ) Hs Sc Sp Dm At Sso Eco RecQ-like helicases RecQ-like RecQ Blm Sgs1 Rqh1 Mus309/DmBlm Wrn RecQL4 RecQ4a Top3a Top3 Top3 Top3 Rmi1 Rmi1/Nec4 Rmi1 Rmi1 Rmi2 Replication-dependent chromatin assembly Hs Sc Sp Dm At Sso Eco CHAF1/CAF1 complex CAF1 complex CAF1 complex CAF1 complex CAF1 complex p150 Rlf2/Cac1 Pcf1 p180 Fas1 p60 Cac2 Pcf2 p105 Fas2 p48 Msi1/Cac3 Pcf3 p55 Msi1 to Msi4 FACT complex FACT complex FACT complex FACT complex FACT complex Supt16h/Spt16 Spt16/Cdc68 Spt16 dre4/spt16 Spt16 Ssrp1 Pob3 Pob3 Ssrp Ssrp1 Nhp6 Nhp6 Asf1a/Cia Asf1 Cia1 Asf1 Asf1a/Sga2 Asf1b/Cia2 Asf1b/Sga1 Nap1L1 to Nap1L5 Nap1 Nap1 Nap1 Nap1 to Nap4 Nrp1 Nrp2 Npm1/nucleoplasmin Nlp/nucleoplasmin Npm2/nucleoplasmin Npm3/nucleoplasmin Nasp Hif1 Sim3 Df31 ACF complex ISW2 complex ACF complex Baz1a/Acf1 Itc1 Acf1 Acf1 Smarca5/Snf2h Isw2 Isw1 RSF complex Hbxap/Rsf1 Smarca5/hSnf2h Chd1 Chd1 Hrp1/Chd1 Chd CHRAC complex CHRAC complex Baz1a/Acf1 Acf1 Smarca5/Snf2h Iswi Chrac1/Chrac15 Top2 Pole3/Chrac17 Chrac-14 Chrac-16 Ihfa, Ihfb H2a (H2afb1, b2, b3, j, v, Hta1, Hta2 Hta1, Hta2 His2A H2a (Hta1, 2, 6, 7, 10, Alba Hua,Hub y, z)e 12, 13) H2afx/H2ax H2ax (Hta3, Hta5) H2afz/H2az Htz1/H2az Htb1 His2Av/H2AZ H2a.z (Hta4, 8, 9, 11) H2b (H2bfm, s, wt) Htb1, Htb2 His2B H2b (Htb1-11) H3 (H3f3a, H3f3c) Hht1, Hht2 Hht1, Hht2 His3 H3.1 (Htr1-3, 9, 11, Cren7 13) H3.3b (H3f3b) Hht3 H3.3 (Htr4-5, 8) H4 (Hist1h4a – Hist1H4l) Hhf1, Hhf2 Hhf1, Hhf2, Hhf3 His4 H4 (Hfo2 – 8) Sul7d H1 (H1fo, nt, oo, x) Hho1 His1 H1 (Hon1, 2, 3) Fis Sister chromatid cohesion Hs Sc Sp Dm At Sso Eco Wdhd1/And-1 Ctf4/Pob1/Chl15 Mcl1 Ctf4 Esco1 Eco1/Ctf7 Eso1 Eco1 Ctf18-RFC clamp loader Ctf18-RFC clamp loader Ctf18-RFC clamp loader Cohesin complex Cohesin complex Cohesin complex Cohesin complex Smc1 Smc1 Psm1 Smc1 Smc1/TTN8 Smc3 Smc3 Psm3 Smc3 Smc3/TTN7 Rad21 Scc1/Mcd1 Rad21 Rad21 Rad21.1, Rad21.2, Rad21.3 Stag1, Stag2 Irr1/Scc3 Psc3 Sa CdcA5/Sororin Dmt/Dalmatian Wfdc5/Wap1 Pds5 Pds5 Pds5 Pds5 DNA damage response Hs Sc Sp Dm At Sso Eco ATM Tel1 Tel1 Tefu/telomere fusion/ATM ATM RecA MRN complex MRX complex MRN complex MRN complex MRN complex MRN complex RecBCD complex 5 Continued DNA damage response (Continued ) 6 Hs Sc Sp Dm At Sso Eco ATR Mec1/Esr1/Sad3 Rad3 Mei-41/Mus-103 ATR RecA Atrip Lcd1/Ddc2/Pie1 Rad26 Mus304 Atrip Chek1/Chk1 Chk1 Chk1/Rad27 Grp/Grapes/Chk1 Chek2/Chk2 Rad53/Lsd1/Mec2/Spk1 Cds1 Lok/Loki/Chk2 Cdc25 Mih1 Cdc25/Sal2 Stg/String/Cdc25 Cdc25-like Checkpoint clamp Checkpoint clamp Checkpoint clamp Checkpoint clamp Checkpoint clamp Rad9 Ddc1 Rad9 Rad9 Rad9 Rad1 Rad17 Rad1 Rad1 Rad1 Hus1 Mec3 Hus1 Hus1 Hus1 Rad17-RFC clamp loader Rad24-RFC clamp loader Rad17-RFC clamp loader Rad17-RFC clamp loader Rad17-RFC clamp loader Ctf18-RFC clamp loader Ctf18-RFC clamp loader Ctf18-RFC clamp loader Tp53/p53 p53 Tp53bp1 Mdm2 Mdm2-like Msh2 Msh2/Pms5 Msh2 Spel1 Msh2 Msh3 Msh3 Swi4 Msh3 Msh6 Msh6/Pms3 Msh6 Msh6 Msh6 Mlh1 Mlh1/Pms2 Mlh1 Dmlh1 Mlh1 Mlh3 Mlh3 Pms1 Pms1 Pms1 Pms1 Pms2 Pms2 Dclre1c/Artemis Brca1 Rad9 Rhp9/Crb2 Brca1 Homologous recombination at stalled replication forks Hs Sc Sp Dm At Sso Eco MRN complex MRX complex MRN complex MRN complex MRN complex MRN complex RecBCD complex Mre11 Mre11 Rad32 Mre11 Mre11 Mre11 RecB Rad50 Rad50 Rad50 Rad50 Rad50 Rad50 RecC Nbs1/Nibrin Xrs2 Nbs1 Nbs1 Nbs1 HerA, NurA RecD Uba2 Sae2 Fub2 Uba2 Sae2 Rad51 Rad51 Rhp51 Spn-a Rad51a, b, c, d RadA RecA Rad52 Rad52 Rhp52/Rad22, Rti1 RecFOR complex REcF RecO RecR Rad54b Rad54 Rhp54 Okr/Okra Rad54 Rad51C Rad55 Rhp55 Rad51c Xrcc3 Rad57 Rhp57 Spn-b Xrcc3 Rad59 Rdh54 Exo1 Exo1 Exo1 Tos/Tosca ExoII FANCi FANCd2 Clamp loaders Hs Sc Sp Dm At Sso Eco RFC clamp loader RFC clamp loader RFC clamp loader RFC clamp loader RFC clamp loader RFC clamp loader Fork clamp loader Rfc1/p140 Rfc1/Cdc44 Rfc1 Rfc140/Gnf1 Rfc1 Rf-CL t1 Rfc2/p40 Rfc2 Rfc2 Rfc40/Rfc2 Rfc2 (Rf-CS)4 t2 Rfc3/p38 Rfc3 Rfc3 Rfc38 Rfc3 t3 Rfc4/p37 Rfc4 Rfc4 Rfc4 Rfc4 d Rfc5/p36 Rfc5 Rfc5 Rfc5 d0 x c Ctf18-RFC clamp loader Ctf18-RFC clamp loader Ctf18-RFC clamp loader Ctf18-RFC clamp loader Ctf18-RFC clamp g-complex loader g1 Chtf18 Ctf18 Ctf18 Cutlet Ctf18 g2 Dcc1 Dcc1 Dcc1 CG11788 g3 Derpc Ctf8 Ctf8 d Rfc2, 3, 4, 5 Rfc2, 3, 4, 5 Rfc2, 3, 4, 5 Rfc3, 4, 38 d0 Rad17-RFC clamp loader Rad24-RFC clamp loader Rad17-RFC clamp loader Rad17-RFC clamp loader Rad17-RFC clamp Rad17 loader Rad17 Rad24 Rad17 Rfc2, 3, 4, 5 Rad17 Rfc2, 3, 4, 5 Rfc2, 3, 4, 5 Rfc2, 3, 4, 5 Rfc2, 3, 4, 5 Elg1-RFC clamp loader Elg1-RFC clamp loader Elg1-RFC clamp loader Atad5 Elg1 Elg1 7 Rfc2, 3, 4, 5 Rfc2, 3, 4, 5 Rfc2, 3, 4, 5 Continued 8 Telomere maintenance Hs Sc Sp Dm At Sso Eco Tert Est2 Trt1 Het-A Tert Tart Tahre Est1A, B, C Est1 Est1 Est1 Cdc13 Est3 Stn1 Stn1 Ten1 Terf1/Trf1 Taz1 Trfl6, Trfl3, Trb1, Trb2, Trfl10, Trfl5, Trfl4, Trfl8, Trb3d Terf2/Trf2 Trfl3, Trb1, Trb2, Trb3, Trfl5, Trfl6, Trfl8, Trfl7, Trfl4, Trfl10d Pot1 Pot1 Pot1 Tinf2/Tin2 TPP1/Tint1/Ptop/Pip1 Rap1 Rap1 Rap1 Tnk1/Tank1 Tnk2/Tank2 Xrcc6/Ku70 Yku70 Pku70 Irbp Ku70, Ku70-like Xrcc5/Ku80 Yku80 Pku80 Ku80 Ku80 Rif1 Rif1 Rif2 SMC5/6 complex Smc5/6 complex SMC5/6 complex Smc5 Smc5 Smc5 Smc5 Smc5 Smc6 Smc6 Smc6 Smc6a, Smc6b Nse1 Nse1 Nse1 Nse2 Mms21/Nse2 Nse2 Mms21 Nse3 Nse3 Nse3 Nse4 Nse4 Nse4/Rad62 Nse5 Nse5 Nse5 Nse6 Kre29/Nse6 Nse6 Linking DNA replication to cell division Hs Sc Sp Dm At Sso Eco CDK
Recommended publications
  • Regulation and Dysregulation of Chromosome Structure in Cancer
    Regulation and Dysregulation of Chromosome Structure in Cancer The MIT Faculty has made this article openly available. Please share how this access benefits you. Your story matters. Citation Hnisz, Denes et al. “Regulation and Dysregulation of Chromosome Structure in Cancer.” Annual Review of Cancer Biology 2, 1 (March 2018): 21–40 © 2018 Annual Reviews As Published https://doi.org/10.1146/annurev-cancerbio-030617-050134 Version Author's final manuscript Citable link http://hdl.handle.net/1721.1/117286 Terms of Use Creative Commons Attribution-Noncommercial-Share Alike Detailed Terms http://creativecommons.org/licenses/by-nc-sa/4.0/ Regulation and dysregulation of chromosome structure in cancer Denes Hnisz1*, Jurian Schuijers1, Charles H. Li1,2, Richard A. Young1,2* 1 Whitehead Institute for Biomedical Research, 455 Main Street, Cambridge, MA 02142, USA 2 Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA * Corresponding authors Corresponding Authors: Denes Hnisz Whitehead Institute for Biomedical Research 455 Main Street Cambridge, MA 02142 Tel: (617) 258-7181 Fax: (617) 258-0376 [email protected] Richard A. Young Whitehead Institute for Biomedical Research 455 Main Street Cambridge, MA 02142 Tel: (617) 258-5218 Fax: (617) 258-0376 [email protected] 1 Summary Cancer arises from genetic alterations that produce dysregulated gene expression programs. Normal gene regulation occurs in the context of chromosome loop structures called insulated neighborhoods, and recent studies have shown that these structures are altered and can contribute to oncogene dysregulation in various cancer cells. We review here the types of genetic and epigenetic alterations that influence neighborhood structures and contribute to gene dysregulation in cancer, present models for insulated neighborhoods associated with the most prominent human oncogenes, and discuss how such models may lead to further advances in cancer diagnosis and therapy.
    [Show full text]
  • Functional Roles of Bromodomain Proteins in Cancer
    cancers Review Functional Roles of Bromodomain Proteins in Cancer Samuel P. Boyson 1,2, Cong Gao 3, Kathleen Quinn 2,3, Joseph Boyd 3, Hana Paculova 3 , Seth Frietze 3,4,* and Karen C. Glass 1,2,4,* 1 Department of Pharmaceutical Sciences, Albany College of Pharmacy and Health Sciences, Colchester, VT 05446, USA; [email protected] 2 Department of Pharmacology, Larner College of Medicine, University of Vermont, Burlington, VT 05405, USA; [email protected] 3 Department of Biomedical and Health Sciences, University of Vermont, Burlington, VT 05405, USA; [email protected] (C.G.); [email protected] (J.B.); [email protected] (H.P.) 4 University of Vermont Cancer Center, Burlington, VT 05405, USA * Correspondence: [email protected] (S.F.); [email protected] (K.C.G.) Simple Summary: This review provides an in depth analysis of the role of bromodomain-containing proteins in cancer development. As readers of acetylated lysine on nucleosomal histones, bromod- omain proteins are poised to activate gene expression, and often promote cancer progression. We examined changes in gene expression patterns that are observed in bromodomain-containing proteins and associated with specific cancer types. We also mapped the protein–protein interaction network for the human bromodomain-containing proteins, discuss the cellular roles of these epigenetic regu- lators as part of nine different functional groups, and identify bromodomain-specific mechanisms in cancer development. Lastly, we summarize emerging strategies to target bromodomain proteins in cancer therapy, including those that may be essential for overcoming resistance. Overall, this review provides a timely discussion of the different mechanisms of bromodomain-containing pro- Citation: Boyson, S.P.; Gao, C.; teins in cancer, and an updated assessment of their utility as a therapeutic target for a variety of Quinn, K.; Boyd, J.; Paculova, H.; cancer subtypes.
    [Show full text]
  • Molecular Profile of Tumor-Specific CD8+ T Cell Hypofunction in a Transplantable Murine Cancer Model
    Downloaded from http://www.jimmunol.org/ by guest on September 25, 2021 T + is online at: average * The Journal of Immunology , 34 of which you can access for free at: 2016; 197:1477-1488; Prepublished online 1 July from submission to initial decision 4 weeks from acceptance to publication 2016; doi: 10.4049/jimmunol.1600589 http://www.jimmunol.org/content/197/4/1477 Molecular Profile of Tumor-Specific CD8 Cell Hypofunction in a Transplantable Murine Cancer Model Katherine A. Waugh, Sonia M. Leach, Brandon L. Moore, Tullia C. Bruno, Jonathan D. Buhrman and Jill E. Slansky J Immunol cites 95 articles Submit online. Every submission reviewed by practicing scientists ? is published twice each month by Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts http://jimmunol.org/subscription Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html http://www.jimmunol.org/content/suppl/2016/07/01/jimmunol.160058 9.DCSupplemental This article http://www.jimmunol.org/content/197/4/1477.full#ref-list-1 Information about subscribing to The JI No Triage! Fast Publication! Rapid Reviews! 30 days* Why • • • Material References Permissions Email Alerts Subscription Supplementary The Journal of Immunology The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2016 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. This information is current as of September 25, 2021. The Journal of Immunology Molecular Profile of Tumor-Specific CD8+ T Cell Hypofunction in a Transplantable Murine Cancer Model Katherine A.
    [Show full text]
  • Initiation of Enzymatic Replication at the Origin of the Escherichia
    Proc. Nati. Acad. Sci. USA Vol. 82, pp. 3954-3958, June 1985 Biochemistry Initiation of enzymatic replication at the origin of the Escherichia coli chromosome: Primase as the sole priming enzyme (DNA/orC/plasmids) ARIE VAN DER ENDEt, TANIA A. BAKER, TOHRU OGAWA*, AND ARTHUR KORNBERG Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305 Contributed by Arthur Kornberg, January 28, 1985 ABSTRACT The enzymatic replication of plasmids con- MATERIALS AND METHODS taining the unique (245 base pair) origin of the Escherichia coli chromosome (oriC) can be initiated with any of three enzyme DNAs and Reagents. pCM959 (4) was a gift from M. Meijer priming systems: primase alone, RNA polymerase alone, or (University of Amsterdam, The Netherlands); pTOA7 (T. both combined (Ogawa, T., Baker, T. A., van der Ende, A. & Ogawa) was constructed by inserting the Hae II-Acc I Kornberg, A. (1985) Proc. Natl. Acad. Sci. USA 82, oriC-containing fragment from M13oriC26 (7) via EcoRI 3562-3566). At certain levels of auxiliary proteins linkers into EcoRI-cleaved pMAPCdSG10, a deletion deriva- (topoisomerase I, protein HU, and RNase H), the solo primase tive of pBR327 (W. A. Segraves, personal communication); system is efficient and responsible for priming synthesis of all pSY317, M13oriC26, M13oriC2LB5, and M13AE101 are DNA strands. Replication of oriC plasmids is here separated described in Table 1 and elsewhere (3, 7). Tricine, creatine into four stages: (i) formation of an isolable, prepriming phosphate, ribo- and deoxyribonucleoside triphosphates complex requiring oriC, dnaA protein, dnaB protein, dnaC (rNTPs and dNTPs) were from Sigma; a-32P-labeled dTTP, protein, gyrase, single-strand binding protein, and ATP; (ii) rATP, rUTP, rGTP, and rCTP (>400 Ci/mmol; 1 Ci = 37 formation of a primed template by primase; (iii) rapid, GBq) were from Amersham.
    [Show full text]
  • Dynamic Molecular Linkers of the Genome: the First Decade of SMC Proteins
    Downloaded from genesdev.cshlp.org on October 8, 2021 - Published by Cold Spring Harbor Laboratory Press REVIEW Dynamic molecular linkers of the genome: the first decade of SMC proteins Ana Losada1 and Tatsuya Hirano2,3 1Spanish National Cancer Center (CNIO), Madrid E-28029, Spain; 2Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA Structural maintenance of chromosomes (SMC) proteins in eukaryotes. The proposed actions of cohesin and con- are chromosomal ATPases, highly conserved from bac- densins offer a plausible, if not complete, explanation for teria to humans, that play fundamental roles in many the sudden appearance of thread-like “substances” (the aspects of higher-order chromosome organization and chromosomes) and their longitudinal splitting during dynamics. In eukaryotes, SMC1 and SMC3 act as the mitosis, first described by Walther Flemming (1882). core of the cohesin complexes that mediate sister chro- Remarkably, SMC proteins are conserved among the matid cohesion, whereas SMC2 and SMC4 function as three phyla of life, indicating that the basic strategy of the core of the condensin complexes that are essential chromosome organization may be evolutionarily con- for chromosome assembly and segregation. Another served from bacteria to humans. An emerging theme is complex containing SMC5 and SMC6 is implicated in that SMC proteins are dynamic molecular linkers of the DNA repair and checkpoint responses. The SMC com- genome that actively fold, tether, and manipulate DNA plexes form unique ring- or V-shaped structures with strands. Their diverse functions range far beyond chro- long coiled-coil arms, and function as ATP-modulated, mosome segregation, and involve nearly all aspects of dynamic molecular linkers of the genome.
    [Show full text]
  • A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
    Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
    [Show full text]
  • DNA Replication Stress Response Involving PLK1, CDC6, POLQ
    DNA replication stress response involving PLK1, CDC6, POLQ, RAD51 and CLASPIN upregulation prognoses the outcome of early/mid-stage non-small cell lung cancer patients C. Allera-Moreau, I. Rouquette, B. Lepage, N. Oumouhou, M. Walschaerts, E. Leconte, V. Schilling, K. Gordien, L. Brouchet, Mb Delisle, et al. To cite this version: C. Allera-Moreau, I. Rouquette, B. Lepage, N. Oumouhou, M. Walschaerts, et al.. DNA replica- tion stress response involving PLK1, CDC6, POLQ, RAD51 and CLASPIN upregulation prognoses the outcome of early/mid-stage non-small cell lung cancer patients. Oncogenesis, Nature Publishing Group: Open Access Journals - Option C, 2012, 1, pp.e30. 10.1038/oncsis.2012.29. hal-00817701 HAL Id: hal-00817701 https://hal.archives-ouvertes.fr/hal-00817701 Submitted on 9 Jun 2021 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Distributed under a Creative Commons Attribution - NonCommercial - NoDerivatives| 4.0 International License Citation: Oncogenesis (2012) 1, e30; doi:10.1038/oncsis.2012.29 & 2012 Macmillan Publishers Limited All rights reserved 2157-9024/12 www.nature.com/oncsis ORIGINAL ARTICLE DNA replication stress response involving PLK1, CDC6, POLQ, RAD51 and CLASPIN upregulation prognoses the outcome of early/mid-stage non-small cell lung cancer patients C Allera-Moreau1,2,7, I Rouquette2,7, B Lepage3, N Oumouhou3, M Walschaerts4, E Leconte5, V Schilling1, K Gordien2, L Brouchet2, MB Delisle1,2, J Mazieres1,2, JS Hoffmann1, P Pasero6 and C Cazaux1 Lung cancer is the leading cause of cancer deaths worldwide.
    [Show full text]
  • Cell Growth-Regulated Expression of Mammalian MCM5 and MCM6 Genes Mediated by the Transcription Factor E2F
    Oncogene (1999) 18, 2299 ± 2309 ã 1999 Stockton Press All rights reserved 0950 ± 9232/99 $12.00 http://www.stockton-press.co.uk/onc Cell growth-regulated expression of mammalian MCM5 and MCM6 genes mediated by the transcription factor E2F Kiyoshi Ohtani1, Ritsuko Iwanaga1, Masataka Nakamura*,1, Masa-aki Ikeda2, Norikazu Yabuta3, Hiromichi Tsuruga3 and Hiroshi Nojima3 1Human Gene Sciences Center, Tokyo Medical and Dental University, Tokyo 113-8510, Japan 2Department of Developmental Biology, Graduate School of Dentistry, Tokyo Medical and Dental University, Tokyo 113-8549, Japan; 3Department of Molecular Genetics, Research Institute for Microbial Diseases, Osaka University, Suita 565-0871, Japan Initiation of DNA replication requires the function of family (MCM2-7) that have been identi®ed in yeast, MCM gene products, which participate in ensuring that Xenopus, and human. Mcm proteins seem to regulate DNA replication occurs only once in the cell cycle. the initiation at the replication origin where the loading Expression of all mammalian genes of the MCM family of the proteins onto the origin recognition complex is induced by growth stimulation, unlike yeast, and the (ORC) is regulated by Cdc6 and cyclin-dependent mRNA levels peak at G1/S boundary. In this study, we kinases (Donovan et al., 1997; Tanaka et al., 1997). examined the transcriptional activities of isolated human However, the mechanism(s) by which Mcm proteins MCM gene promoters. Human MCM5 and MCM6 control the initiation of DNA replication remains promoters with mutation in the E2F sites failed in unclear. promoter regulation following serum stimulation and Xenopus Mcm proteins seem to be able to access exogenous E2F expression.
    [Show full text]
  • Supplementary Table S5. Differentially Expressed Gene Lists of PD-1High CD39+ CD8 Tils According to 4-1BB Expression Compared to PD-1+ CD39- CD8 Tils
    BMJ Publishing Group Limited (BMJ) disclaims all liability and responsibility arising from any reliance Supplemental material placed on this supplemental material which has been supplied by the author(s) J Immunother Cancer Supplementary Table S5. Differentially expressed gene lists of PD-1high CD39+ CD8 TILs according to 4-1BB expression compared to PD-1+ CD39- CD8 TILs Up- or down- regulated genes in Up- or down- regulated genes Up- or down- regulated genes only PD-1high CD39+ CD8 TILs only in 4-1BBneg PD-1high CD39+ in 4-1BBpos PD-1high CD39+ CD8 compared to PD-1+ CD39- CD8 CD8 TILs compared to PD-1+ TILs compared to PD-1+ CD39- TILs CD39- CD8 TILs CD8 TILs IL7R KLRG1 TNFSF4 ENTPD1 DHRS3 LEF1 ITGA5 MKI67 PZP KLF3 RYR2 SIK1B ANK3 LYST PPP1R3B ETV1 ADAM28 H2AC13 CCR7 GFOD1 RASGRP2 ITGAX MAST4 RAD51AP1 MYO1E CLCF1 NEBL S1PR5 VCL MPP7 MS4A6A PHLDB1 GFPT2 TNF RPL3 SPRY4 VCAM1 B4GALT5 TIPARP TNS3 PDCD1 POLQ AKAP5 IL6ST LY9 PLXND1 PLEKHA1 NEU1 DGKH SPRY2 PLEKHG3 IKZF4 MTX3 PARK7 ATP8B4 SYT11 PTGER4 SORL1 RAB11FIP5 BRCA1 MAP4K3 NCR1 CCR4 S1PR1 PDE8A IFIT2 EPHA4 ARHGEF12 PAICS PELI2 LAT2 GPRASP1 TTN RPLP0 IL4I1 AUTS2 RPS3 CDCA3 NHS LONRF2 CDC42EP3 SLCO3A1 RRM2 ADAMTSL4 INPP5F ARHGAP31 ESCO2 ADRB2 CSF1 WDHD1 GOLIM4 CDK5RAP1 CD69 GLUL HJURP SHC4 GNLY TTC9 HELLS DPP4 IL23A PITPNC1 TOX ARHGEF9 EXO1 SLC4A4 CKAP4 CARMIL3 NHSL2 DZIP3 GINS1 FUT8 UBASH3B CDCA5 PDE7B SOGA1 CDC45 NR3C2 TRIB1 KIF14 TRAF5 LIMS1 PPP1R2C TNFRSF9 KLRC2 POLA1 CD80 ATP10D CDCA8 SETD7 IER2 PATL2 CCDC141 CD84 HSPA6 CYB561 MPHOSPH9 CLSPN KLRC1 PTMS SCML4 ZBTB10 CCL3 CA5B PIP5K1B WNT9A CCNH GEM IL18RAP GGH SARDH B3GNT7 C13orf46 SBF2 IKZF3 ZMAT1 TCF7 NECTIN1 H3C7 FOS PAG1 HECA SLC4A10 SLC35G2 PER1 P2RY1 NFKBIA WDR76 PLAUR KDM1A H1-5 TSHZ2 FAM102B HMMR GPR132 CCRL2 PARP8 A2M ST8SIA1 NUF2 IL5RA RBPMS UBE2T USP53 EEF1A1 PLAC8 LGR6 TMEM123 NEK2 SNAP47 PTGIS SH2B3 P2RY8 S100PBP PLEKHA7 CLNK CRIM1 MGAT5 YBX3 TP53INP1 DTL CFH FEZ1 MYB FRMD4B TSPAN5 STIL ITGA2 GOLGA6L10 MYBL2 AHI1 CAND2 GZMB RBPJ PELI1 HSPA1B KCNK5 GOLGA6L9 TICRR TPRG1 UBE2C AURKA Leem G, et al.
    [Show full text]
  • 2020 Program Book
    PROGRAM BOOK Note that TAGC was cancelled and held online with a different schedule and program. This document serves as a record of the original program designed for the in-person meeting. April 22–26, 2020 Gaylord National Resort & Convention Center Metro Washington, DC TABLE OF CONTENTS About the GSA ........................................................................................................................................................ 3 Conference Organizers ...........................................................................................................................................4 General Information ...............................................................................................................................................7 Mobile App ....................................................................................................................................................7 Registration, Badges, and Pre-ordered T-shirts .............................................................................................7 Oral Presenters: Speaker Ready Room - Camellia 4.......................................................................................7 Poster Sessions and Exhibits - Prince George’s Exhibition Hall ......................................................................7 GSA Central - Booth 520 ................................................................................................................................8 Internet Access ..............................................................................................................................................8
    [Show full text]
  • 1 AGING Supplementary Table 2
    SUPPLEMENTARY TABLES Supplementary Table 1. Details of the eight domain chains of KIAA0101. Serial IDENTITY MAX IN COMP- INTERFACE ID POSITION RESOLUTION EXPERIMENT TYPE number START STOP SCORE IDENTITY LEX WITH CAVITY A 4D2G_D 52 - 69 52 69 100 100 2.65 Å PCNA X-RAY DIFFRACTION √ B 4D2G_E 52 - 69 52 69 100 100 2.65 Å PCNA X-RAY DIFFRACTION √ C 6EHT_D 52 - 71 52 71 100 100 3.2Å PCNA X-RAY DIFFRACTION √ D 6EHT_E 52 - 71 52 71 100 100 3.2Å PCNA X-RAY DIFFRACTION √ E 6GWS_D 41-72 41 72 100 100 3.2Å PCNA X-RAY DIFFRACTION √ F 6GWS_E 41-72 41 72 100 100 2.9Å PCNA X-RAY DIFFRACTION √ G 6GWS_F 41-72 41 72 100 100 2.9Å PCNA X-RAY DIFFRACTION √ H 6IIW_B 2-11 2 11 100 100 1.699Å UHRF1 X-RAY DIFFRACTION √ www.aging-us.com 1 AGING Supplementary Table 2. Significantly enriched gene ontology (GO) annotations (cellular components) of KIAA0101 in lung adenocarcinoma (LinkedOmics). Leading Description FDR Leading Edge Gene EdgeNum RAD51, SPC25, CCNB1, BIRC5, NCAPG, ZWINT, MAD2L1, SKA3, NUF2, BUB1B, CENPA, SKA1, AURKB, NEK2, CENPW, HJURP, NDC80, CDCA5, NCAPH, BUB1, ZWILCH, CENPK, KIF2C, AURKA, CENPN, TOP2A, CENPM, PLK1, ERCC6L, CDT1, CHEK1, SPAG5, CENPH, condensed 66 0 SPC24, NUP37, BLM, CENPE, BUB3, CDK2, FANCD2, CENPO, CENPF, BRCA1, DSN1, chromosome MKI67, NCAPG2, H2AFX, HMGB2, SUV39H1, CBX3, TUBG1, KNTC1, PPP1CC, SMC2, BANF1, NCAPD2, SKA2, NUP107, BRCA2, NUP85, ITGB3BP, SYCE2, TOPBP1, DMC1, SMC4, INCENP. RAD51, OIP5, CDK1, SPC25, CCNB1, BIRC5, NCAPG, ZWINT, MAD2L1, SKA3, NUF2, BUB1B, CENPA, SKA1, AURKB, NEK2, ESCO2, CENPW, HJURP, TTK, NDC80, CDCA5, BUB1, ZWILCH, CENPK, KIF2C, AURKA, DSCC1, CENPN, CDCA8, CENPM, PLK1, MCM6, ERCC6L, CDT1, HELLS, CHEK1, SPAG5, CENPH, PCNA, SPC24, CENPI, NUP37, FEN1, chromosomal 94 0 CENPL, BLM, KIF18A, CENPE, MCM4, BUB3, SUV39H2, MCM2, CDK2, PIF1, DNA2, region CENPO, CENPF, CHEK2, DSN1, H2AFX, MCM7, SUV39H1, MTBP, CBX3, RECQL4, KNTC1, PPP1CC, CENPP, CENPQ, PTGES3, NCAPD2, DYNLL1, SKA2, HAT1, NUP107, MCM5, MCM3, MSH2, BRCA2, NUP85, SSB, ITGB3BP, DMC1, INCENP, THOC3, XPO1, APEX1, XRCC5, KIF22, DCLRE1A, SEH1L, XRCC3, NSMCE2, RAD21.
    [Show full text]
  • Noelia Díaz Blanco
    Effects of environmental factors on the gonadal transcriptome of European sea bass (Dicentrarchus labrax), juvenile growth and sex ratios Noelia Díaz Blanco Ph.D. thesis 2014 Submitted in partial fulfillment of the requirements for the Ph.D. degree from the Universitat Pompeu Fabra (UPF). This work has been carried out at the Group of Biology of Reproduction (GBR), at the Department of Renewable Marine Resources of the Institute of Marine Sciences (ICM-CSIC). Thesis supervisor: Dr. Francesc Piferrer Professor d’Investigació Institut de Ciències del Mar (ICM-CSIC) i ii A mis padres A Xavi iii iv Acknowledgements This thesis has been made possible by the support of many people who in one way or another, many times unknowingly, gave me the strength to overcome this "long and winding road". First of all, I would like to thank my supervisor, Dr. Francesc Piferrer, for his patience, guidance and wise advice throughout all this Ph.D. experience. But above all, for the trust he placed on me almost seven years ago when he offered me the opportunity to be part of his team. Thanks also for teaching me how to question always everything, for sharing with me your enthusiasm for science and for giving me the opportunity of learning from you by participating in many projects, collaborations and scientific meetings. I am also thankful to my colleagues (former and present Group of Biology of Reproduction members) for your support and encouragement throughout this journey. To the “exGBRs”, thanks for helping me with my first steps into this world. Working as an undergrad with you Dr.
    [Show full text]