ANNUAL REPORT for July 2004 – June 2005

Total Page:16

File Type:pdf, Size:1020Kb

ANNUAL REPORT for July 2004 – June 2005 ANNUAL REPORT for July 2004 – June 2005 RESEARCH COLLABORATORY FOR STRUCTURAL BIOINFORMATICS: Rutgers, The State University of New Jersey San Diego Supercomputer Center, University of California, San Diego About the Cover The data that the RCSB PDB tracks from structural genomics projects – from target selection to structure determination – are illustrated here. The structures shown are from the nine pilot centers participating in the first phase of the NIH-funded Protein Structure Initiative. 1nkt Crystal structure of the SecA protein 1t3u translocation ATPase4 (interior) Mycobacterium tuberculosis Unknown conserved bacterial (TB) Structural 1rjj protein from Pseudomonas Genomics Consortium Solution structure of a aeruginosa PAO1 homodimeric hypothet- New York Structural ical protein from Genomics Research Arabidopsis thaliana1 1nc7 Consortium Center for Eukaryotic Crystal structure of Structural Genomics Thermotoga 1sq4 maritima 1070 Crystal structure of Midwest Center for the putative Structural Genomics glyoxylate induced protein from Pseudomonas aeruginosa Northeast Structural Genomics Consortium 1xn4 Putative Mar1 ribonuclease from Leishmania major Structural Genomics of Pathogenic Protozoa Consortium 1n0e Crystal structure of a cell division and cell wall biosynthesis protein 1o4v UPF0040 from Crystal structure of phospho- Mycoplasma pneumoniae 5 ribosylaminoimidazole Berkeley Structural mutase PurE (Tm0446) from 1pry 3 Genomics Center Thermotoga maritima Structure determination of Joint Center for fibrillarin homologue from Structural Genomics hyperthermophilic archaeon Pyrococcus furiosus2 Southeast Collaboratory for Contents Structural Genomics About the Cover . .2 Data Query and Reporting . .9 Message from the Director . .3 PDBML/XML Data Uniformity Files . .10 What is the RCSB PDB? . .4 Time-stamped Copies of PDB Archives . .10 PDB Users . .4 Browsing for Structures... .10 The RCSB PDB Team Mission . .5 Related Resources . .11 RCSB PDB Management . .5 Structural Genomics . .11 Funding . .5 Physical Archives . .11 wwPDB . .6 Recent Publications . .11 Advisory Committee . .6 Data Dictionaries: mmCIF and PDB . .12 RCSB PDB Services: Data Deposition . .7 NMR Structures . .12 Data Input: Deposition, Validation, and Annotation . .7 Community Interactions . .12-13 Software for Deposition and Validation . .7 Molecule of the Month Series . .13 Statistics . .8 Other Educational Resources . .13 Annotators work to represent PDB data... .8 Workshops . .14 ADIT Depositions . .8 Important Web Addresses & Help Desks . .14 RCSB PDB Services: Data Query, Reporting and Access . .9 References . .15 Data Distribution and Access . .9 2 RCSB PDB Annual Report Message from the Director The RCSB PDB is uniquely positioned to track the growth of structural biology. In terms of shear volume, the numbers are impressive. More than one hundred structures are deposited every week, each with its own story to tell. Some come from small laboratories that focus on a single aspect of biology aimed at cracking the mystery of how proteins function. Others come from structural genomics groups where high throughput methods make it possible to rapidly determine structures on a genomic scale and give us an even broader view of the many possible shapes of proteins. Now we can see structures of large macro- molecular machines that have been determined using a combi- nation of powerful methods, including cryo-electron microscopy. The RCSB PDB is up to the challenge of handling the data produced by all of these initiatives with methods for managing both its volume and complexity. It is both daunting and excit- ing to be part of this era in which the secrets of biology are being revealed at the molecular level. The RCSB is not alone in managing the data from these new initiatives. Through the worldwide PDB (wwPDB) we are working with our partners in Japan (the PDBj) and Europe (MSD-EBI) to ensure that the data remain uniform and freely available. This report presents the many different RCSB PDB activities in data deposition, data access and education. We hope you find that it reflects the excitement we feel about our contribution to the burgeoning field of structural biology. Helen M. Berman Director, RCSB PDB 1y0q Golden, B. L., Kim, H., Chase, E.: (2005) Crystal Structure of a phage Twort group I ribozyme-product complex. Nat Struct Mol Biol 12, 82-89. July 2004 – June 2005 3 What is the RCSB PDB? SNAPSHOT – July 1, 2005 31535 released atomic coordinate entries The structures housed in the PDB range from small pieces of Molecule Type protein or DNA to complex machines, such as viruses and 28739 proteins, peptides, and viruses ribosomes. Each molecule plays a part in at least one biological 1481 nucleic acids process and each has value in helping scientists unravel the 1302 protein/nucleic acid complexes mysteries of life. Their structural shapes provide insight about 13 carbohydrates fundamental biological processes and in some cases, about disease Experimental Technique or drug interactions. 26932 diffraction and other 4603 NMR The PDB archives include a wide variety of medically important structures, including enzymes and other proteins associated with influenza, HIV, SARS and other viruses; parts of prion pro- The RCSB stores these data in a relational database that can be teins (including the bovine form implicated in Mad Cow accessed using several different tools for searching and creating Disease); the amyloid peptide associated with Alzheimer’s graphical reports. The RCSB PDB website also offers other disease; and the p53 tumor-suppressor protein associated with a resources for associated aspects of structural biology, including wide variety of human cancers. structural genomics, data representation formats, and down- loadable software. The website includes a variety of The information in the PDB about materials for learning about structural biology these biological macromole- and the PDB, and for interacting with cules holds significant the multifaceted interests of the promise for the PDB user communities. pharmaceutical and biotechnology Data residing in the PDB industries in the results from research projects search for new all over the world. In recog- drugs and in the nition of the truly interna- effort to understand the tional nature of the PDB mystery of human disease. and the critical importance of maintaining that data in a single The data stored in the PDB archive, the worldwide PDB (wwPDB) 8 include the three-dimensional was established in 2003 . All wwPDB coordinates for the structures of sites share responsibilities for data these biological macromolecules deposition, processing, and distribution of the PDB archives, and support the standardization of structure data that have been determined experimen- 1u0n tally using X-ray crystallography, Fukuda, K., Doggett, T., (see also page 6). Laurenzi, I. J., Liddington, NMR, and cryo-electron microscopy. R. C., Diacovo, T. G. Understanding what these structures (2005) The snake venom PDB Users look like and being able to ‘see’ how protein botrocetin acts as a biological brace to promote As the sole repository for three-dimensional structure data of they bind to various ligands greatly aids dysfunctional platelet aggre- biological macromolecules, the PDB is a critical resource for in understanding how they function. gation. Nat Struct Mol Biol 12, 152-159. academic, pharmaceutical, and biotechnology research. Structural biologists in industry and academia who focus on The importance of the data related to experimental structure determinations work with wwPDB staff three-dimensional structures was recognized early in the history to make these data available in the archives. Researchers from a of structural biology. The scientific community felt strongly wide variety of disciplines then use these data in their own that these data needed to be freely available to people in all studies, which can range from structural genomics to computa- fields of research. As a result, in 1971 the Protein Data Bank tional biology to structural biology and beyond. (PDB) was founded at Brookhaven National Laboratory6 as the sole international repository for three-dimensional structure Students and teachers also depend upon the RCSB PDB's collec- data of biological macromolecules. In 1999, management was tion of resources to help elucidate various subjects related to bio- assumed by the non-profit consortium the Research Collaboratory logical structure. Resources available include RCSB tools to find for Structural Bioinformatics7. and visualize proteins, an education-centered webpage with materials for all levels of understanding, and the popular This online repository contains the coordinates and related Molecule of the Month feature that regularly highlights different information for more than 31,000 structures. molecules from the PDB (page 13). 4 RCSB PDB Annual Report What is the RCSB PDB? RCSB PDB Management The RCSB PDB is managed by Rutgers, The State University of New Jersey and the San Diego Supercomputer Center (SDSC), an organized research unit of the University of California, San Diego (UCSD) – two member institutions of the RCSB. The group from the Center for Advanced Research in Biotechnology/University of Maryland Biotechnology Institute/National Institute of Standards and Technology is no longer part of the RCSB consortium. The Project Leaders manage the overall operations. Helen M. Berman, a Board of Governors Professor of Chemistry and Chemical Biology at Rutgers, is the Director of the RCSB
Recommended publications
  • Fibrillarin from Archaea to Human
    Biol. Cell (2015) 107, 1–16 DOI: 10.1111/boc.201400077 Review Fibrillarin from Archaea to human Ulises Rodriguez-Corona*, Margarita Sobol†, Luis Carlos Rodriguez-Zapata‡, Pavel Hozak† and Enrique Castano*1 *Unidad de Bioquımica´ y Biologıa´ molecular de plantas, Centro de Investigacion´ Cientıfica´ de Yucatan,´ Colonia Chuburna´ de Hidalgo, Merida,´ Yucatan, Mexico, †Department of Biology of the Cell Nucleus, Institute of Molecular Genetics of the Academy of Sciences of the Czech Republic, Prague 14220, Czech Republic, and ‡Unidad de Biotecnologıa,´ Centro de Investigacion´ Cientıfica´ de Yucatan,´ Colonia Chuburna´ de Hidalgo, Merida,´ Yucatan, Mexico Fibrillarin is an essential protein that is well known as a molecular marker of transcriptionally active RNA polyme- rase I. Fibrillarin methyltransferase activity is the primary known source of methylation for more than 100 methylated sites involved in the first steps of preribosomal processing and required for structural ribosome stability. High expression levels of fibrillarin have been observed in several types of cancer cells, particularly when p53 levels are reduced, because p53 is a direct negative regulator of fibrillarin transcription. Here, we show fibrillarin domain conservation, structure and interacting molecules in different cellular processes as well as with several viral proteins during virus infection. Additional supporting information may be found in the online version of this article at the publisher’s web-site Introduction progression, senescence and biogenesis of small nu- The nucleolus is the largest visible structure inside clear RNA and tRNAs proliferation and many forms the cell nucleus. It exists both as a dynamic and sta- of stress response (Andersen et al., 2005; Hinsby ble region depending of the nature and amount of et al., 2006; Boisvert et al., 2007; Shaw and Brown, the molecules that it is made of.
    [Show full text]
  • The Nucleolus – a Gateway to Viral Infection? Brief Review
    Arch Virol (2002) 147: 1077–1089 DOI 10.1007/s00705-001-0792-0 The nucleolus – a gateway to viral infection? Brief Review J. A. Hiscox School of Animal and Microbial Sciences, University of Reading, U.K. Received August 24, 2001; accepted December 26, 2001 Published online March 18, 2002, © Springer-Verlag 2002 Summary. A number of viruses and viral proteins interact with a dynamic sub- nuclear structure called the nucleolus. The nucleolus is present during interphase in mammalian cells and is the site of ribosome biogenesis, and has been implicated in controlling regulatory processes such as the cell cycle. Viruses interact with the nucleolus and its antigens; viral proteins co-localise with factors such as nucleolin, B23 and fibrillarin, and can cause their redistribution during infection. Viruses can use these components as part of their replication process, and also use the nucleolus as a site of replication itself. Many of these properties are not restricted to any particular type of virus or replication mechanism, and examples of these processes can be found in DNA, RNA and retroviruses. Evidence suggests that viruses may target the nucleolus and its components to favour viral transcription, translation and perhaps alter the cell cycle in order to promote virus replication. Autoimmunity to nucleolin and fibrillarin have been associated with a number of diseases, and by targeting the nucleolus and displacing nucleolar antigens, virus infection might play a role in the initiation of these conditions. Introduction The eukaryotic nucleus contains a number of domains or subcompartments, which include nucleoli, nuclear Cajal bodies, nuclear speckles, transcription and replica- tion foci, and chromosome territories [34].
    [Show full text]
  • DDX5 Targets Tissue-Specific Rnas to Promote Intestine Tumorigenesis
    bioRxiv preprint doi: https://doi.org/10.1101/2020.03.25.006668; this version posted March 26, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. DDX5 targets tissue-specific RNAs to promote intestine tumorigenesis Nazia Abbasi1,4, Tianyun Long1,4, Yuxin Li1, Evelyn Ma1, Brian A. Yee1, Parth R. Patel1, Ibrahim M SayeD2, Nissi Varki2, Soumita Das2, PraDipta Ghosh1, 3, Gene W. Yeo1, WenDy J.M. Huang1,5 1 Department of Cellular anD Molecular MeDicine, University of California San Diego, La Jolla, CA 2 Department of Pathology, University of California San Diego, La Jolla, CA 3 Department of MeDicine, University of California San Diego, La Jolla, CA 4 These authors contributeD equally 5 CorresponDing author email: [email protected] Abstract Tumorigenesis in Different segments of the intestinal tract involves tissue-specific oncogenic Drivers. In the colon, complement component 3 (C3) activation is a major contributor to inflammation anD malignancies. By contrast, tumorigenesis in the small intestine involves fatty aciD-binding protein 1 (FABP1). However, little is known of the upstream mechanisms Driving their expressions in Different segments of the intestinal tract. Here, we report that an RNA binDing protein DDX5 augments C3 and FABP1 expressions post-transcriptionally to promote tumorigenesis in the colon anD small intestine, respectively. Mice with epithelial-specific knockout of DDX5 are protecteD from intestine tumorigenesis. The iDentification of DDX5 as the common upstream regulator of tissue-specific oncogenic molecules proviDes a new therapeutic target for intestine cancers.
    [Show full text]
  • Utpa and Utpb Chaperone Nascent Pre-Ribosomal RNA and U3 Snorna to Initiate Eukaryotic Ribosome Assembly
    ARTICLE Received 6 Apr 2016 | Accepted 27 May 2016 | Published 29 Jun 2016 DOI: 10.1038/ncomms12090 OPEN UtpA and UtpB chaperone nascent pre-ribosomal RNA and U3 snoRNA to initiate eukaryotic ribosome assembly Mirjam Hunziker1,*, Jonas Barandun1,*, Elisabeth Petfalski2, Dongyan Tan3, Cle´mentine Delan-Forino2, Kelly R. Molloy4, Kelly H. Kim5, Hywel Dunn-Davies2, Yi Shi4, Malik Chaker-Margot1,6, Brian T. Chait4, Thomas Walz5, David Tollervey2 & Sebastian Klinge1 Early eukaryotic ribosome biogenesis involves large multi-protein complexes, which co-transcriptionally associate with pre-ribosomal RNA to form the small subunit processome. The precise mechanisms by which two of the largest multi-protein complexes—UtpA and UtpB—interact with nascent pre-ribosomal RNA are poorly understood. Here, we combined biochemical and structural biology approaches with ensembles of RNA–protein cross-linking data to elucidate the essential functions of both complexes. We show that UtpA contains a large composite RNA-binding site and captures the 50 end of pre-ribosomal RNA. UtpB forms an extended structure that binds early pre-ribosomal intermediates in close proximity to architectural sites such as an RNA duplex formed by the 50 ETS and U3 snoRNA as well as the 30 boundary of the 18S rRNA. Both complexes therefore act as vital RNA chaperones to initiate eukaryotic ribosome assembly. 1 Laboratory of Protein and Nucleic Acid Chemistry, The Rockefeller University, New York, New York 10065, USA. 2 Wellcome Trust Centre for Cell Biology, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, UK. 3 Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.
    [Show full text]
  • Broad Susceptibility of Nucleolar Proteins and Autoantigens to Complement C1 Protease Degradation
    Broad Susceptibility of Nucleolar Proteins and Autoantigens to Complement C1 Protease Degradation This information is current as Yitian Cai, Seng Yin Kelly Wee, Junjie Chen, Boon Heng of September 25, 2021. Dennis Teo, Yee Leng Carol Ng, Khai Pang Leong and Jinhua Lu J Immunol published online 25 October 2017 http://www.jimmunol.org/content/early/2017/10/25/jimmun ol.1700728 Downloaded from Supplementary http://www.jimmunol.org/content/suppl/2017/10/25/jimmunol.170072 Material 8.DCSupplemental http://www.jimmunol.org/ Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication by guest on September 25, 2021 *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2017 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. Published October 25, 2017, doi:10.4049/jimmunol.1700728 The Journal of Immunology Broad Susceptibility of Nucleolar Proteins and Autoantigens to Complement C1 Protease Degradation Yitian Cai,*,1 Seng Yin Kelly Wee,*,1 Junjie Chen,* Boon Heng Dennis Teo,* Yee Leng Carol Ng,† Khai Pang Leong,† and Jinhua Lu* Anti-nuclear autoantibodies, which frequently target the nucleoli, are pathogenic hallmarks of systemic lupus erythematosus (SLE).
    [Show full text]
  • Dual Function of C/D Box Small Nucleolar Rnas in Rrna PNAS PLUS Modification and Alternative Pre-Mrna Splicing
    Dual function of C/D box small nucleolar RNAs in rRNA PNAS PLUS modification and alternative pre-mRNA splicing Marina Falaleevaa, Amadis Pagesb, Zaneta Matuszeka, Sana Hidmic, Lily Agranat-Tamirc, Konstantin Korotkova, Yuval Nevod, Eduardo Eyrasb,e, Ruth Sperlingc, and Stefan Stamma,1 aDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY 40536; bDepartment of Experimental and Health Sciences, Universitat Pompeu Fabra, E08003 Barcelona, Spain; cDepartment of Genetics, Hebrew University of Jerusalem, 91904 Jerusalem, Israel; dDepartment of Microbiology and Molecular Genetics, Computation Center at the Hebrew University and Hadassah Medical Center, 91904 Jerusalem, Israel; and eCatalan Institution for Research and Advanced Studies, E08010 Barcelona, Spain Edited by James E. Dahlberg, University of Wisconsin Medical School, Madison, WI, and approved February 5, 2016 (received for review October 1, 2015) C/D box small nucleolar RNAs (SNORDs) are small noncoding RNAs, SNORD fragments are not microRNAs, which have an average and their best-understood function is to target the methyltrans- length of 21–22 nt (13–16), and suggests that these fragments may ferase fibrillarin to rRNA (for example, SNORD27 performs 2′-O- have additional functions. methylation of A27 in 18S rRNA). Unexpectedly, we found a subset The association of some SNORDs with specific diseases sug- of SNORDs, including SNORD27, in soluble nuclear extract made gests that they may possess functions in addition to directing the under native conditions, where fibrillarin was not detected, indi- 2′-O-methylation of rRNA. For example, the loss of SNORD116 cating that a fraction of the SNORD27 RNA likely forms a protein expression is a decisive factor in Prader–Willi syndrome, the most complex different from canonical snoRNAs found in the insoluble common genetic cause for hyperphagia and obesity (17, 18).
    [Show full text]
  • Anti-Fibrillarin Antibody (ARG10749)
    Product datasheet [email protected] ARG10749 Package: 50 μl anti-Fibrillarin antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes Fibrillarin Tested Reactivity Hu, Ms, Rat, Mk Tested Application ICC/IF, IHC-Fr, WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name Fibrillarin Antigen Species Human Immunogen Full length Human Fibrillarin expressed in and purified from E. coli. Conjugation Un-conjugated Alternate Names rRNA 2'-O-methyltransferase fibrillarin; RNU3IP1; 34 kDa nucleolar scleroderma antigen; FIB; FLRN; EC 2.1.1.-; Histone-glutamine methyltransferase Application Instructions Application table Application Dilution ICC/IF 1:2000 - 1:5000 IHC-Fr Assay-dependent WB 1:2000 - 1:5000 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Calculated Mw 34 kDa Properties Form Liquid Purification Affinity purification. Buffer PBS and 50% Glycerol. Stabilizer 50% Glycerol Concentration 1 mg/ml Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. Note For laboratory research only, not for drug, diagnostic or other use. www.arigobio.com 1/3 Bioinformation Gene Symbol FBL Gene Full Name fibrillarin Background This gene product is a component of a nucleolar small nuclear ribonucleoprotein (snRNP) particle thought to participate in the first step in processing preribosomal RNA. It is associated with the U3, U8, and U13 small nuclear RNAs and is located in the dense fibrillar component (DFC) of the nucleolus.
    [Show full text]
  • Rpl13a Small Nucleolar Rnas Regulate Systemic Glucose Metabolism
    RESEARCH ARTICLE The Journal of Clinical Investigation Rpl13a small nucleolar RNAs regulate systemic glucose metabolism Jiyeon Lee,1 Alexis N. Harris,1 Christopher L. Holley,1 Jana Mahadevan,2 Kelly D. Pyles,1 Zeno Lavagnino,3 David E. Scherrer,1 Hideji Fujiwara,1 Rohini Sidhu,1 Jessie Zhang,1 Stanley Ching-Cheng Huang,4 David W. Piston,3 Maria S. Remedi,2 Fumihiko Urano,2 Daniel S. Ory,1 and Jean E. Schaffer1 1Diabetic Cardiovascular Disease Center and Department of Internal Medicine, 2Department of Internal Medicine, 3Department of Cell Biology and Physiology and Department of Internal Medicine, and 4Department of Pathology and Immunology, Washington University School of Medicine in St. Louis, St. Louis, Missouri, USA. Small nucleolar RNAs (snoRNAs) are non-coding RNAs that form ribonucleoproteins to guide covalent modifications of ribosomal and small nuclear RNAs in the nucleus. Recent studies have also uncovered additional non-canonical roles for snoRNAs. However, the physiological contributions of these small RNAs are largely unknown. Here, we selectively deleted four snoRNAs encoded within the introns of the ribosomal protein L13a (Rpl13a) locus in a mouse model. Loss of Rpl13a snoRNAs altered mitochondrial metabolism and lowered reactive oxygen species tone, leading to increased glucose- stimulated insulin secretion from pancreatic islets and enhanced systemic glucose tolerance. Islets from mice lacking Rpl13a snoRNAs demonstrated blunted oxidative stress responses. Furthermore, these mice were protected against diabetogenic stimuli that cause oxidative stress damage to islets. Our study illuminates a previously unrecognized role for snoRNAs in metabolic regulation. Introduction predicted ribosomal RNA targets and that the Rpl13a snoRNAs Box C/D snoRNAs are short noncoding RNAs containing conserved accumulate in the cytosol during oxidative stress suggest that C and D box consensus motifs that form ribonucleoproteins with the Rpl13a snoRNAs may function through noncanonical mecha- NOP56, NOP58, 15.5 kDa, and the methyltransferase fibrillarin (1).
    [Show full text]
  • Active Liquid-Like Behavior of Nucleoli Determines Their Size and Shape in Xenopus Laevis Oocytes
    Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes Clifford P. Brangwynnea,b,c,1,2, Timothy J. Mitchisonc,d, and Anthony A. Hymana aMax Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany; bMax Planck Institute for the Physics of Complex Systems, Nöthnitzerstrasse 38, 01187 Dresden, Germany; cMarine Biological Laboratory, 7 MBL Street, Woods Hole, MA, 02543; and dDepartment of Systems Biology, Harvard Medical School, 200 Longwood Avenue, Boston, MA, 02115 Edited by Dirk Görlich, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany, and accepted by the Editorial Board January 27, 2011 (received for review November 16, 2010) For most intracellular structures with larger than molecular dimen- Nucleoli are essential RNA/protein bodies within the nucleus sions, little is known about the connection between underlying that function primarily as factories for ribosome subunit biogen- molecular activities and higher order organization such as size esis. Ribosome production is critical for rapid cell growth, and and shape. Here, we show that both the size and shape of the tissue pathologists use the size, number, and shape of nucleoli amphibian oocyte nucleolus ultimately arise because nucleoli as indicators of cancer growth and malignancy (5, 6). Nucleoli behave as liquid-like droplets of RNA and protein, exhibiting char- consist of hundreds of different RNA and protein components, acteristic viscous fluid dynamics even on timescales of <1 min. We including many ATP-hydrolyzing RNA helicases (7). Ribosome use these dynamics to determine an apparent nucleolar viscosity, precursors are thought to be assembled and modified during and we show that this viscosity is ATP-dependent, suggesting a radial transport away from a central core of tandem ribosomal role for active processes in fluidizing internal contents.
    [Show full text]
  • A Small Nucleolar RNA Is Processed from an Intron of the Human Gene Encoding Ribosomal Protein $3
    Downloaded from genesdev.cshlp.org on October 6, 2021 - Published by Cold Spring Harbor Laboratory Press A small nucleolar RNA is processed from an intron of the human gene encoding ribosomal protein $3 Kazimierz Tyc Tycowski, Mei-Di Shu, and Joan A. Steitz Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06536-0812 USA A human small nucleolar RNA, identified previously in HeLa cells by anti-fibrillarin autoantibody precipitation and termed RNA X, has been characterized. It comprises two uridine-rich variants (148 and 146 nucleotides}, which we refer to as snRNA U15A and U15B. Secondary structure models predict for both variants a U15-specific stem-loop structure, as well as a new structural motif that contains conserved sequences and can also be recognized in the other fibrillarin-associated nucleolar snRNAs, U3, U14, and RNA Y. The single-copy gene for human U15A has been found unexpectedly to reside in intron 1 of the ribosomal protein $3 gene; the U15A sequence appears on the same strand as the $3 mRNA and does not exhibit canonical transcription signals for nuclear RNA polymerases. U15A RNA is processed in vitro from $3 intron 1 transcripts to yield the correct 5' end with a 5'-monophosphate; the in vitro system requires ATP for 3' cleavage, which occurs a few nucleotides downstream of the mature end. The production of a single primary transcript specifying the mRNA for a ribosomal or nucleolar protein and a nucleolar snRNA may constitute a general mechanism for balancing the levels of nucleolar components in vertebrate cells.
    [Show full text]
  • Signature in Peripheral Blood Neutrophils Periodontitis
    Periodontitis Associates with a Type 1 IFN Signature in Peripheral Blood Neutrophils Helen J. Wright, John B. Matthews, Iain L. C. Chapple, Nic Ling-Mountford and Paul R. Cooper This information is current as of September 23, 2021. J Immunol 2008; 181:5775-5784; ; doi: 10.4049/jimmunol.181.8.5775 http://www.jimmunol.org/content/181/8/5775 Downloaded from References This article cites 72 articles, 11 of which you can access for free at: http://www.jimmunol.org/content/181/8/5775.full#ref-list-1 Why The JI? Submit online. http://www.jimmunol.org/ • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication *average by guest on September 23, 2021 Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2008 by The American Association of Immunologists All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Periodontitis Associates with a Type 1 IFN Signature in Peripheral Blood Neutrophils1 Helen J. Wright, John B. Matthews, Iain L. C. Chapple, Nic Ling-Mountford, and Paul R. Cooper2 Peripheral blood neutrophils from periodontitis patients exhibit a hyperreactive and hyperactive phenotype (collectively termed hyperresponsivity) in terms of production of reactive oxygen species (ROS).
    [Show full text]
  • Supplementary Table 1
    Up-regulated accession # Development M93275 ADFP, adipose differentiation related protein D43694 MATH-1, homolog of atonal 1 M64068 Bmi-1, zinc finger protein AW124785 Midnolin, midbrain nucleolar protein AI843178 Cla3, Cerebellar ataxia 3 D10712 Nedd1, Neural precursor cell expressed, developmentally down-regulated gene 1 AB011678 Doublecortin, for neurogenesis M57683 mPDGF-alpha-R, PDGF alpha receptor U41626 DSS1, deleted in split hand/split foot 1 homolog (Dss1), for limb development AB010833 PTCH2, patched 2, Mouse homolog of yeast CDC46 NP_034226 Ebf3, early B-cell factor 3 AI846695 Qk, Quaking U63386 Edr1 Early development regulator 1 (homolog of polyhomeotic 1), Mph1 AI043016 Rnf2, Ring finger protein 2 X69942 Enhancer-trap-locus 1, for transcription regulation AF100694 Ruvbl1, Ruv-B like protein 1, DNA helicase AW123618 Fzd2, Frizzled homolog 2 U88566 Sfrp1, secreted frizzled related protein 1 AA681520 Geminin-pending, for embryogenesis and morphogenesis U88567 Sfrp2, secreted frizzled related protein 2 AB025922 Gli1, GLI-Kruppel family member 1 AF089721 Smo, Smoothened X99104 Gli2, GLI-Kruppel family member 2 AF009414 SOX11, SRY-box containing gene 11 U61362 Grg1, groucho-related gene 1, Tle1, transducin-like enhancer of split 1 U85614 SRG3, Smarcc1, SWI/SNF related, matrix associated, action dependent regulator of chromatin, subfamily, member 1 M97506 Hen1, helix-loop-helix protein AI837838 Tmeff1, Transmembrane protein with EGF-like and two follistatin-like domains 1 U79748 Madh4, MAD homolog 4, for transcription regulation
    [Show full text]