SANTA CRUZ BIOTECHNOLOGY, INC. DDX50 Shrna (M) Lentiviral Particles: Sc-142942-V

Total Page:16

File Type:pdf, Size:1020Kb

SANTA CRUZ BIOTECHNOLOGY, INC. DDX50 Shrna (M) Lentiviral Particles: Sc-142942-V SANTA CRUZ BIOTECHNOLOGY, INC. DDX50 shRNA (m) Lentiviral Particles: sc-142942-V BACKGROUND APPLICATIONS DDX50 (Probable ATP-dependent RNA helicase DDX50, Nucleolar protein DDX50 shRNA (m) Lentiviral Particles is recommended for the inhibition of Gu2, Gu-β) is a 737 amino acid protein encoded by the human gene DDX50. DDX50 expression in mouse cells. DDX50 belongs to the DEAD box helicase family, DDX21/DDX50 subfamily and contains one helicase ATP-binding domain and one C-terminal helicase SUPPORT REAGENTS domain. DDX50 is a functional interaction partner of c-Jun in human cells. Control shRNA Lentiviral Particles: sc-108080. Available as 200 µl frozen The N-terminal transcription activation region of c-Jun interacts with a C-ter- viral stock containing 1.0 x 106 infectious units of virus (IFU); contains an minal domain of DDX50. This interaction is stimulated by anisomycin treat- shRNA construct encoding a scrambled sequence that will not lead to the ment in a manner that is concurrent with, but independent of, c-Jun phos- specific degradation of any known cellular mRNA. phorylation. DDX50 is also believed to be a probable ATP-dependent RNA helicase. RNA helicases are highly conserved enzymes that utilize the ener- RT-PCR REAGENTS gy derived from NTP hydrolysis to modulate the structure of RNA. RNA heli- cases participate in all biological processes that involve RNA, including tran- Semi-quantitative RT-PCR may be performed to monitor DDX50 gene expres- scription, splicing and translation. sion knockdown using RT-PCR Primer: DDX50 (m)-PR: sc-142942-PR (20 µl). Annealing temperature for the primers should be 55-60° C and the extension REFERENCES temperature should be 68-72° C. 1. Doorbar, J., et al. 2000. The E1E4 protein of human papillomavirus type 16 BIOSAFETY associates with a putative RNA helicase through sequences in its C termi- nus. J. Virol. 74: 10081-10095. Lentiviral particles can be employed in standard Biosafety Level 2 tissue culture facilities (and should be treated with the same level of caution as 2. Bhattacharya, R., et al. 2002. Methylphosphate cap structure in small RNAs with any other potentially infectious reagent). Lentiviral particles are repli- reduces the affinity of RNAs to La protein. Gene Expr. 10: 243-253. cation-incompetent and are designed to self-inactivate after transduction 3. Valdez, B.C., et al. 2002. Expression, cellular localization, and enzymatic and integration of shRNA constructs into genomic DNA of target cells. activities of RNA helicase II/Guβ. Exp. Cell Res. 276: 249-263. RESEARCH USE 4. Westermarck, J., et al. 2002. The DEXD/H-box RNA helicase RHII/Gu is a co-factor for c-Jun-activated transcription. EMBO J. 21: 451-460. The purchase of this product conveys to the buyer the nontransferable right to use the purchased amount of the product and all replicates and derivatives 5. Regard, J.B., et al. 2004. Verge: a novel vascular early response gene. J. for research purposes conducted by the buyer in his laboratory only (whether Neurosci. 24: 4092-4103. the buyer is an academic or for-profit entity). The buyer cannot sell or other- wise transfer (a) this product (b) its components or (c) materials made using CHROMOSOMAL LOCATION this product or its components to a third party, or otherwise use this product Genetic locus: Ddx50 (mouse) mapping to 10 B4. or its components or materials made using this product or its components for Commercial Purposes. PRODUCT DDX50 shRNA (m) Lentiviral Particles are concentrated, transduction-ready viral particles containing a target-specific construct that encodes a 19-25 nt (plus hairpin) shRNA designed to knock down gene expression. Each vial con- tains 200 µl frozen stock containing 1.0 x 106 infectious units of virus (IFU) in Dulbecco’s Modified Eagle’s Medium with 25 mM HEPES pH 7.3. Suitable for 10-20 transductions. Also see DDX50 siRNA (m): sc-142942 and DDX50 shRNA Plasmid (m): sc-142942-SH as alternate gene silencing products. STORAGE Store lentiviral particles at -80º C. Stable for at least one year from the date of shipment. Once thawed, particles can be stored at 4º C for up to one week. Avoid repeated freeze thaw cycles. PROTOCOLS See our web site at www.scbt.com for detailed protocols and support products. Santa Cruz Biotechnology, Inc. 1.800.457.3801 831.457.3800 fax 831.457.3801 Europe +00800 4573 8000 49 6221 4503 0 www.scbt.com.
Recommended publications
  • Solution Structure of the GUCT Domain from Human RNA Helicase II/Gu[Beta]
    proteins STRUCTURE O FUNCTION O BIOINFORMATICS Solution structure of the GUCT domain from human RNA helicase II/Gub reveals the RRM fold, but implausible RNA interactions Satoshi Ohnishi,1 Kimmo Pa¨a¨kko¨nen,1 Seizo Koshiba,1 Naoya Tochio,1 Manami Sato,1 Naohiro Kobayashi,1 Takushi Harada,1 Satoru Watanabe,1 Yutaka Muto,1 Peter Gu¨ntert,1 Akiko Tanaka,1 Takanori Kigawa,1,2 and Shigeyuki Yokoyama1,3* 1 Systems and Structural Biology Center, RIKEN, Tsurumi, Yokohama 230-0045, Japan 2 Department of Computational Intelligence and Systems Science, Interdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, Midori-ku, Yokohama 226-8503, Japan 3 Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan INTRODUCTION ABSTRACT a a a a Human RNA helicase II/Gu (RH-II/Gu or Deadbox Human RNA helicase II/Gu (RH-II/Gu ) and RNA helicase protein 21) is a multifunctional enzyme that unwinds dou- II/Gub (RH-II/Gub) are paralogues that share the same ble-stranded RNA in the 50 to 30 direction and folds single- domain structure, consisting of the DEAD box helicase 1–5 domain (DEAD), the helicase conserved C-terminal domain stranded RNA in an ATP-dependent manner. These (helicase_C), and the GUCT domain. The N-terminal regions RNA-unwinding and RNA-folding activities are independ- of the RH-II/Gu proteins, including the DEAD domain and ent, and they reside in distinct regions of the protein. The the helicase_C domain, unwind double-stranded RNAs. The RNA helicase activity is catalyzed by the N-terminal three- 1 C-terminal tail of RH-II/Gua, which follows the GUCT do- quarters of the molecule in the presence of Mg2 , where as main, folds a single RNA strand, while that of RH-II/Gub the RNA-foldase activity is located in the C-terminal region 1 does not, and the GUCT domain is not essential for either and functions in a Mg2 independent manner.2 As shown the RNA helicase or foldase activity.
    [Show full text]
  • Nucleolin and Its Role in Ribosomal Biogenesis
    NUCLEOLIN: A NUCLEOLAR RNA-BINDING PROTEIN INVOLVED IN RIBOSOME BIOGENESIS Inaugural-Dissertation zur Erlangung des Doktorgrades der Mathematisch-Naturwissenschaftlichen Fakultät der Heinrich-Heine-Universität Düsseldorf vorgelegt von Julia Fremerey aus Hamburg Düsseldorf, April 2016 2 Gedruckt mit der Genehmigung der Mathematisch-Naturwissenschaftlichen Fakultät der Heinrich-Heine-Universität Düsseldorf Referent: Prof. Dr. A. Borkhardt Korreferent: Prof. Dr. H. Schwender Tag der mündlichen Prüfung: 20.07.2016 3 Die vorgelegte Arbeit wurde von Juli 2012 bis März 2016 in der Klinik für Kinder- Onkologie, -Hämatologie und Klinische Immunologie des Universitätsklinikums Düsseldorf unter Anleitung von Prof. Dr. A. Borkhardt und in Kooperation mit dem ‚Laboratory of RNA Molecular Biology‘ an der Rockefeller Universität unter Anleitung von Prof. Dr. T. Tuschl angefertigt. 4 Dedicated to my family TABLE OF CONTENTS 5 TABLE OF CONTENTS TABLE OF CONTENTS ............................................................................................... 5 LIST OF FIGURES ......................................................................................................10 LIST OF TABLES .......................................................................................................12 ABBREVIATION .........................................................................................................13 ABSTRACT ................................................................................................................19 ZUSAMMENFASSUNG
    [Show full text]
  • Long First Exons and Epigenetic Marks Distinguish Conserved Pachytene
    ARTICLE https://doi.org/10.1038/s41467-020-20345-3 OPEN Long first exons and epigenetic marks distinguish conserved pachytene piRNA clusters from other mammalian genes ✉ Tianxiong Yu 1,2,7, Kaili Fan 1,2,7, Deniz M. Özata 3, Gen Zhang4,YuFu 2,5,6, William E. Theurkauf4 , ✉ ✉ Phillip D. Zamore 3 & Zhiping Weng 1,2 – 1234567890():,; In the male germ cells of placental mammals, 26 30-nt-long PIWI-interacting RNAs (piR- NAs) emerge when spermatocytes enter the pachytene phase of meiosis. In mice, pachytene piRNAs derive from ~100 discrete autosomal loci that produce canonical RNA polymerase II transcripts. These piRNA clusters bear 5′ caps and 3′ poly(A) tails, and often contain introns that are removed before nuclear export and processing into piRNAs. What marks pachytene piRNA clusters to produce piRNAs, and what confines their expression to the germline? We report that an unusually long first exon (≥ 10 kb) or a long, unspliced transcript correlates with germline-specific transcription and piRNA production. Our integrative analysis of tran- scriptome, piRNA, and epigenome datasets across multiple species reveals that a long first exon is an evolutionarily conserved feature of pachytene piRNA clusters. Furthermore, a highly methylated promoter, often containing a low or intermediate level of CG dinucleotides, correlates with germline expression and somatic silencing of pachytene piRNA clusters. Pachytene piRNA precursor transcripts bind THOC1 and THOC2, THO complex subunits known to promote transcriptional elongation and mRNA nuclear export. Together, these features may explain why the major sources of pachytene piRNA clusters specifically gen- erate these unique small RNAs in the male germline of placental mammals.
    [Show full text]
  • The Function and Evolution of C2H2 Zinc Finger Proteins and Transposons
    The function and evolution of C2H2 zinc finger proteins and transposons by Laura Francesca Campitelli A thesis submitted in conformity with the requirements for the degree of Doctor of Philosophy Department of Molecular Genetics University of Toronto © Copyright by Laura Francesca Campitelli 2020 The function and evolution of C2H2 zinc finger proteins and transposons Laura Francesca Campitelli Doctor of Philosophy Department of Molecular Genetics University of Toronto 2020 Abstract Transcription factors (TFs) confer specificity to transcriptional regulation by binding specific DNA sequences and ultimately affecting the ability of RNA polymerase to transcribe a locus. The C2H2 zinc finger proteins (C2H2 ZFPs) are a TF class with the unique ability to diversify their DNA-binding specificities in a short evolutionary time. C2H2 ZFPs comprise the largest class of TFs in Mammalian genomes, including nearly half of all Human TFs (747/1,639). Positive selection on the DNA-binding specificities of C2H2 ZFPs is explained by an evolutionary arms race with endogenous retroelements (EREs; copy-and-paste transposable elements), where the C2H2 ZFPs containing a KRAB repressor domain (KZFPs; 344/747 Human C2H2 ZFPs) are thought to diversify to bind new EREs and repress deleterious transposition events. However, evidence of the gain and loss of KZFP binding sites on the ERE sequence is sparse due to poor resolution of ERE sequence evolution, despite the recent publication of binding preferences for 242/344 Human KZFPs. The goal of my doctoral work has been to characterize the Human C2H2 ZFPs, with specific interest in their evolutionary history, functional diversity, and coevolution with LINE EREs.
    [Show full text]
  • DDX50 (Human) Recombinant Protein (P01)
    DDX50 (Human) Recombinant Protein (P01) Catalog # : H00079009-P01 規格 : [ 10 ug ] [ 25 ug ] List All Specification Application Image Product Human DDX50 full-length ORF ( NP_076950.1, 1 a.a. - 737 a.a.) Enzyme-linked Immunoabsorbent Assay Description: recombinant protein with GST-tag at N-terminal. Western Blot (Recombinant Sequence: MPGKLLWGDIMELEAPLEESESQKKERQKSDRRKSRHHYDSDEKSETR protein) ENGVTDDLDAPKAKKSKMKEKLNGDTEEGFNRLSDEFSKSHKSRRKDLP NGDIDEYEKKSKRVSSLDTSTHKSSDNKLEETLTREQKEGAFSNFPISEE Antibody Production TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERL QRNQETIKKSRSPKVLVLAPTRELANQVAKDFKDITRKLSVACFYGGTSY Protein Array QSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGF AEQVEDIIHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQVD LVGKMTQKAATTVEHLAIQCHWSQRPAVIGDVLQVYSGSEGRAIIFCETK KNVTEMAMNPHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAA RGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICICFYQPRERGQ LRYVEQKAGITFKRVGVPSTMDLVKSKSMDAIRSLASVSYAAVDFFRPSA QRLIEEKGAVDALAAALAHISGASSFEPRSLITSDKGFVTMTLESLEEIQD VSCAWKELNRKLSSNAVSQITRMCLLKGNMGVCFDVPTTESERLQAEW HDSDWILSVPAKLPEIEEYYDGNTSSNSRQRSGWSSGRSGRSGRSGGR SGGRSGRQSRQGSRSGSRQDGRRRSGNRNRSRSGGHKRSFD Host: Wheat Germ (in vitro) Theoretical MW 109 (kDa): Preparation in vitro wheat germ expression system Method: Purification: Glutathione Sepharose 4 Fast Flow Quality Control 12.5% SDS-PAGE Stained with Coomassie Blue. Testing: Storage Buffer: 50 mM Tris-HCI, 10 mM reduced Glutathione, pH=8.0 in the elution buffer. Storage Store at -80°C. Aliquot to avoid repeated freezing and thawing. Instruction: Note: Best use within three
    [Show full text]
  • Identification of RNA-Binding Protein LARP4B As a Tumor Suppressor in Glioma
    Published OnlineFirst March 1, 2016; DOI: 10.1158/0008-5472.CAN-15-2308 Cancer Molecular and Cellular Pathobiology Research Identification of RNA-Binding Protein LARP4B as a Tumor Suppressor in Glioma Hideto Koso1, Hungtsung Yi1, Paul Sheridan2, Satoru Miyano2, Yasushi Ino3, Tomoki Todo3, and Sumiko Watanabe1 Abstract Transposon-based insertional mutagenesis is a valuable patient-derived glioma stem cell populations. The expression method for conducting unbiased forward genetic screens to levels of CDKN1A and BAX were also upregulated upon identify cancer genes in mice. We used this system to elucidate LARP4B overexpression, and the growth-inhibitory effects were factors involved in the malignant transformation of neural partially dependent on p53 (TP53) activity in cells expressing stem cells into glioma-initiating cells. We identified an RNA- wild-type, but not mutant, p53. We further found that the La binding protein, La-related protein 4b (LARP4B), as a candi- module, which is responsible for the RNA chaperone activity date tumor-suppressor gene in glioma. LARP4B expression was of LARP4B, was important for the growth-suppressive effect consistently decreased in human glioma stem cells and cell and was associated with BAX mRNA. Finally, LARP4B deple- lines compared with normal neural stem cells. Moreover, tion in p53 and Nf1-deficient mouse primary astrocytes pro- heterozygous deletion of LARP4B was detected in nearly moted cell proliferation and led to increased tumor size and 80% of glioblastomas in The Cancer Genome Atlas database. invasiveness in xenograft and orthotopic models. These data LARP4B loss was also associated with low expression and poor provide strong evidence that LARP4B serves as a tumor-sup- patient survival.
    [Show full text]
  • A Catalogue of Stress Granules' Components
    Catarina Rodrigues Nunes A Catalogue of Stress Granules’ Components: Implications for Neurodegeneration UNIVERSIDADE DO ALGARVE Departamento de Ciências Biomédicas e Medicina 2019 Catarina Rodrigues Nunes A Catalogue of Stress Granules’ Components: Implications for Neurodegeneration Master in Oncobiology – Molecular Mechanisms of Cancer This work was done under the supervision of: Clévio Nóbrega, Ph.D UNIVERSIDADE DO ALGARVE Departamento de Ciências Biomédicas e Medicina 2019 i ii A catalogue of Stress Granules’ Components: Implications for neurodegeneration Declaração de autoria de trabalho Declaro ser a autora deste trabalho, que é original e inédito. Autores e trabalhos consultados estão devidamente citados no texto e constam na listagem de referências incluída. I declare that I am the author of this work, that is original and unpublished. Authors and works consulted are properly cited in the text and included in the list of references. _______________________________ (Catarina Nunes) iii Copyright © 2019 Catarina Nunes A Universidade do Algarve reserva para si o direito, em conformidade com o disposto no Código do Direito de Autor e dos Direitos Conexos, de arquivar, reproduzir e publicar a obra, independentemente do meio utilizado, bem como de a divulgar através de repositórios científicos e de admitir a sua cópia e distribuição para fins meramente educacionais ou de investigação e não comerciais, conquanto seja dado o devido crédito ao autor e editor respetivos. iv Part of the results of this thesis were published in Nunes,C.; Mestre,I.; Marcelo,A. et al. MSGP: the first database of the protein components of the mammalian stress granules. Database (2019) Vol. 2019. (In annex A). v vi ACKNOWLEDGEMENTS A realização desta tese marca o final de uma etapa académica muito especial e que jamais irei esquecer.
    [Show full text]
  • DEAH)/RNA Helicase a Helicases Sense Microbial DNA in Human Plasmacytoid Dendritic Cells
    Aspartate-glutamate-alanine-histidine box motif (DEAH)/RNA helicase A helicases sense microbial DNA in human plasmacytoid dendritic cells Taeil Kima, Shwetha Pazhoora, Musheng Baoa, Zhiqiang Zhanga, Shino Hanabuchia, Valeria Facchinettia, Laura Bovera, Joel Plumasb, Laurence Chaperotb, Jun Qinc, and Yong-Jun Liua,1 aDepartment of Immunology, Center for Cancer Immunology Research, University of Texas M. D. Anderson Cancer Center, Houston, TX 77030; bDepartment of Research and Development, Etablissement Français du Sang Rhône-Alpes Grenoble, 38701 La Tronche, France; and cDepartment of Biochemistry, Baylor College of Medicine, Houston, TX 77030 Edited by Ralph M. Steinman, The Rockefeller University, New York, NY, and approved July 14, 2010 (received for review May 10, 2010) Toll-like receptor 9 (TLR9) senses microbial DNA and triggers type I Microbial nucleic acids, including their genomic DNA/RNA IFN responses in plasmacytoid dendritic cells (pDCs). Previous and replicating intermediates, work as strong PAMPs (13), so studies suggest the presence of myeloid differentiation primary finding PRR-sensing pathogenic nucleic acids and investigating response gene 88 (MyD88)-dependent DNA sensors other than their signaling pathway is of general interest. Cytosolic RNA is TLR9 in pDCs. Using MS, we investigated C-phosphate-G (CpG)- recognized by RLRs, including RIG-I, melanoma differentiation- binding proteins from human pDCs, pDC-cell lines, and interferon associated gene 5 (MDA5), and laboratory of genetics and physi- regulatory factor 7 (IRF7)-expressing B-cell lines. CpG-A selectively ology 2 (LGP2). RIG-I senses 5′-triphosphate dsRNA and ssRNA bound the aspartate-glutamate-any amino acid-aspartate/histi- or short dsRNA with blunt ends.
    [Show full text]
  • Frac-Seq Reveals Isoform-Specific Recruitment to Polyribosomes
    Downloaded from genome.cshlp.org on September 29, 2021 - Published by Cold Spring Harbor Laboratory Press Research Frac-seq reveals isoform-specific recruitment to polyribosomes Timothy Sterne-Weiler,1,4 Rocio Teresa Martinez-Nunez,2,4 Jonathan M. Howard,2 Ivan Cvitovik,2 Sol Katzman,3 Muhammad A. Tariq,1 Nader Pourmand,1 and Jeremy R. Sanford2,5 1Biomolecular Engineering Department, Jack Baskin School of Engineering, University of California Santa Cruz, Santa Cruz, California 95064, USA; 2Department of Molecular, Cellular and Developmental Biology, University of California Santa Cruz, Santa Cruz, California 95064, USA; 3Center for Biomolecular Science and Engineering, University of California Santa Cruz, Santa Cruz, California 95064, USA Pre-mRNA splicing is required for the accurate expression of virtually all human protein coding genes. However, splicing also plays important roles in coordinating subsequent steps of pre-mRNA processing such as polyadenylation and mRNA export. Here, we test the hypothesis that nuclear pre-mRNA processing influences the polyribosome association of al- ternative mRNA isoforms. By comparing isoform ratios in cytoplasmic and polyribosomal extracts, we determined that the alternative products of ~30% (597/1954) of mRNA processing events are differentially partitioned between these subcellular fractions. Many of the events exhibiting isoform-specific polyribosome association are highly conserved across mammalian genomes, underscoring their possible biological importance. We find that differences in polyribosome as- sociation may be explained, at least in part by the observation that alternative splicing alters the cis-regulatory landscape of mRNAs isoforms. For example, inclusion or exclusion of upstream open reading frames (uORFs) in the 59UTR as well as Alu-elements and microRNA target sites in the 39UTR have a strong influence on polyribosome association of alternative mRNA isoforms.
    [Show full text]
  • DDX50 Maxpab Mouse Polyclonal Antibody (B01)
    DDX50 MaxPab mouse polyclonal Storage Instruction: Store at -20°C or lower. Aliquot to antibody (B01) avoid repeated freezing and thawing. Entrez GeneID: 79009 Catalog Number: H00079009-B01 Gene Symbol: DDX50 Regulatory Status: For research use only (RUO) Gene Alias: GU2, GUB, MGC3199, RH-II/GuB Product Description: Mouse polyclonal antibody raised against a full-length human DDX50 protein. Gene Summary: DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are Immunogen: DDX50 (NP_076950.1, 1 a.a. ~ 737 a.a) putative RNA helicases. They are implicated in a number full-length human protein. of cellular processes involving alteration of RNA Sequence: secondary structure such as translation initiation, nuclear MPGKLLWGDIMELEAPLEESESQKKERQKSDRRKSR and mitochondrial splicing, and ribosome and HHYDSDEKSETRENGVTDDLDAPKAKKSKMKEKLNG spliceosome assembly. Based on their distribution DTEEGFNRLSDEFSKSHKSRRKDLPNGDIDEYEKKSK patterns, some members of this DEAD box protein family RVSSLDTSTHKSSDNKLEETLTREQKEGAFSNFPISEE are believed to be involved in embryogenesis, TIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTG spermatogenesis, and cellular growth and division. This KTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELAN gene encodes a DEAD box enzyme that may be QVAKDFKDITRKLSVACFYGGTSYQSQINHIRNGIDILV involved in ribosomal RNA synthesis or processing. This GTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFA gene and DDX21, also called RH-II/GuA, have similar EQVEDIIHESYKTDSEDNPQTLLFSATCPQWVYKVAKK genomic structures and are in tandem orientation on YMKSRYEQVDLVGKMTQKAATTVEHLAIQCHWSQRP
    [Show full text]
  • DNMT3L Is a Regulator of X Chromosome Compaction and Post-Meiotic Gene Transcription
    DNMT3L Is a Regulator of X Chromosome Compaction and Post-Meiotic Gene Transcription Natasha M. Zamudio1,2, Hamish S. Scott4, Katja Wolski1, Chi-Yi Lo1, Charity Law5,6, Dillon Leong5, Sarah A. Kinkel5,7, Suyinn Chong6, Damien Jolley3, Gordon K. Smyth5, David de Kretser1, Emma Whitelaw6, Moira K. O’Bryan1,2* 1 The Department of Anatomy and Developmental Biology, Monash University, Victoria, Australia, 2 The Australian Research Council Centre of Excellence in Biotechnology and Development, Monash University, Victoria, Australia, 3 The Monash Institute of Health Services Research, Monash University, Victoria, Australia, 4 The Institute of Medical and Veterinary Science, University of Adelaide, Adelaide, Australia, 5 The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia, 6 Queensland Institute of Medical Research, Herston, Queensland, Australia, 7 Department of Medical Biology, University of Melbourne, Victoria, Australia Abstract Previous studies on the epigenetic regulator DNA methyltransferase 3-Like (DNMT3L), have demonstrated it is an essential regulator of paternal imprinting and early male meiosis. Dnmt3L is also a paternal effect gene, i.e., wild type offspring of heterozygous mutant sires display abnormal phenotypes suggesting the inheritance of aberrant epigenetic marks on the paternal chromosomes. In order to reveal the mechanisms underlying these paternal effects, we have assessed X chromosome meiotic compaction, XY chromosome aneuploidy rates and global transcription in meiotic and haploid germ cells from male mice heterozygous for Dnmt3L. XY bodies from Dnmt3L heterozygous males were significantly longer than those from wild types, and were associated with a three-fold increase in XY bearing sperm. Loss of a Dnmt3L allele resulted in deregulated expression of a large number of both X-linked and autosomal genes within meiotic cells, but more prominently in haploid germ cells.
    [Show full text]
  • Tissue-Specific Disallowance of Housekeeping Genes
    Downloaded from genome.cshlp.org on September 29, 2021 - Published by Cold Spring Harbor Laboratory Press Tissue-specific disallowance of housekeeping genes: the other face of cell differentiation Lieven Thorrez1,2,4, Ilaria Laudadio3, Katrijn Van Deun4, Roel Quintens1,4, Nico Hendrickx1,4, Mikaela Granvik1,4, Katleen Lemaire1,4, Anica Schraenen1,4, Leentje Van Lommel1,4, Stefan Lehnert1,4, Cristina Aguayo-Mazzucato5, Rui Cheng-Xue6, Patrick Gilon6, Iven Van Mechelen4, Susan Bonner-Weir5, Frédéric Lemaigre3, and Frans Schuit1,4,$ 1 Gene Expression Unit, Dept. Molecular Cell Biology, Katholieke Universiteit Leuven, 3000 Leuven, Belgium 2 ESAT-SCD, Department of Electrical Engineering, Katholieke Universiteit Leuven, 3000 Leuven, Belgium 3 Université Catholique de Louvain, de Duve Institute, 1200 Brussels, Belgium 4 Center for Computational Systems Biology, Katholieke Universiteit Leuven, 3000 Leuven, Belgium 5 Section of Islet Transplantation and Cell Biology, Joslin Diabetes Center, Harvard University, Boston, MA 02215, US 6 Unité d’Endocrinologie et Métabolisme, University of Louvain Faculty of Medicine, 1200 Brussels, Belgium $ To whom correspondence should be addressed: Frans Schuit O&N1 Herestraat 49 - bus 901 3000 Leuven, Belgium Email: [email protected] Phone: +32 16 347227 , Fax: +32 16 345995 Running title: Disallowed genes Keywords: disallowance, tissue-specific, tissue maturation, gene expression, intersection-union test Abbreviations: UTR UnTranslated Region H3K27me3 Histone H3 trimethylation at lysine 27 H3K4me3 Histone H3 trimethylation at lysine 4 H3K9ac Histone H3 acetylation at lysine 9 BMEL Bipotential Mouse Embryonic Liver Downloaded from genome.cshlp.org on September 29, 2021 - Published by Cold Spring Harbor Laboratory Press Abstract We report on a hitherto poorly characterized class of genes which are expressed in all tissues, except in one.
    [Show full text]