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  • 1
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    Principles of ubiquitin and SUMO modifications in DNA repair (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-03-28
    Description: With the discovery in the late 1980s that the DNA-repair gene RAD6 encodes a ubiquitin-conjugating enzyme, it became clear that protein modification by ubiquitin conjugation has a much broader significance than had previously been assumed. Now, two decades later, ubiquitin and its cousin SUMO are implicated in a range of human diseases, including breast cancer and Fanconi anaemia, giving fresh momentum to studies focused on the relationships between ubiquitin, SUMO and DNA-repair pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bergink, Steven -- Jentsch, Stefan -- England -- Nature. 2009 Mar 26;458(7237):461-7. doi: 10.1038/nature07963.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19325626" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *DNA Repair ; Humans ; Phosphorylation ; Proliferating Cell Nuclear Antigen/metabolism ; SUMO-1 Protein/*metabolism ; Ubiquitin/*metabolism ; Ubiquitination
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Varshavsky's contributions (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baumeister, Wolfgang -- Bachmair, Andreas -- Chau, Vincent -- Cohen, Robert -- Coffino, Phil -- Demartino, George -- Deshaies, Raymond -- Dohmen, Juergen -- Emr, Scott -- Finley, Daniel -- Hampton, Randy -- Hill, Christopher -- Hochstrasser, Mark -- Huber, Robert -- Jackson, Peter -- Jentsch, Stefan -- Johnson, Erica -- Kwon, Yong Tae -- Pagano, Michele -- Pickart, Cecile -- Rechsteiner, Martin -- Scheffner, Martin -- Sommer, Thomas -- Tansey, William -- Tyers, Mike -- Vierstra, Richard -- Weissman, Allan -- Wilkinson, Keith D -- Wolf, Dieter -- New York, N.Y. -- Science. 2004 Nov 19;306(5700):1290-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15550643" target="_blank"〉PubMed〈/a〉
    Keywords: History, 20th Century ; History, 21st Century ; Nobel Prize ; Proteasome Endopeptidase Complex/*metabolism ; Proteins/metabolism ; Ubiquitin/*metabolism ; Ubiquitin-Protein Ligase Complexes/genetics/*metabolism ; United States
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Role of the ubiquitin-like protein Hub1 in splice-site usage and alternative splicing (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-05-27
    Description: Alternative splicing of pre-messenger RNAs diversifies gene products in eukaryotes and is guided by factors that enable spliceosomes to recognize particular splice sites. Here we report that alternative splicing of Saccharomyces cerevisiae SRC1 pre-mRNA is promoted by the conserved ubiquitin-like protein Hub1. Structural and biochemical data show that Hub1 binds non-covalently to a conserved element termed HIND, which is present in the spliceosomal protein Snu66 in yeast and mammals, and Prp38 in plants. Hub1 binding mildly alters spliceosomal protein interactions and barely affects general splicing in S. cerevisiae. However, spliceosomes that lack Hub1, or are defective in Hub1-HIND interaction, cannot use certain non-canonical 5' splice sites and are defective in alternative SRC1 splicing. Hub1 confers alternative splicing not only when bound to HIND, but also when experimentally fused to Snu66, Prp38, or even the core splicing factor Prp8. Our study indicates a novel mechanism for splice site utilization that is guided by non-covalent modification of the spliceosome by an unconventional ubiquitin-like modifier.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3587138/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3587138/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mishra, Shravan Kumar -- Ammon, Tim -- Popowicz, Grzegorz M -- Krajewski, Marcin -- Nagel, Roland J -- Ares, Manuel Jr -- Holak, Tad A -- Jentsch, Stefan -- GM040478/GM/NIGMS NIH HHS/ -- R01 GM040478/GM/NIGMS NIH HHS/ -- England -- Nature. 2011 May 25;474(7350):173-8. doi: 10.1038/nature10143.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21614000" target="_blank"〉PubMed〈/a〉
    Keywords: *Alternative Splicing ; Amino Acid Sequence ; Binding Sites ; Cell Line ; Gene Deletion ; *Gene Expression Regulation, Fungal ; Humans ; Ligases/deficiency/genetics/*metabolism ; Membrane Proteins/genetics ; Models, Molecular ; Molecular Sequence Data ; Nuclear Proteins/genetics ; Protein Binding ; Protein Conformation ; RNA Splice Sites/*genetics ; RNA, Fungal/*genetics/metabolism ; RNA, Messenger/genetics/metabolism ; Ribonucleoprotein, U4-U6 Small Nuclear/deficiency/genetics ; Ribonucleoprotein, U5 Small Nuclear/deficiency/genetics ; Ribonucleoproteins, Small Nuclear/chemistry/deficiency/genetics/metabolism ; Saccharomyces cerevisiae/chemistry/*genetics/*metabolism ; Saccharomyces cerevisiae Proteins/chemistry/genetics/*metabolism ; Schizosaccharomyces/chemistry/genetics/metabolism ; Schizosaccharomyces pombe Proteins/genetics/metabolism ; Spliceosomes/chemistry/metabolism ; Ubiquitin-Protein Ligase Complexes/deficiency/genetics/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 4
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    When proteins receive deadly messages at birth (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jentsch, S -- New York, N.Y. -- Science. 1996 Feb 16;271(5251):955-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zentrum fur Molekulare Biologie, Universitat Heidelberg, Germany. Jentsch@sun0.urz.uni-heidelberg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8584931" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Codon, Terminator ; Endopeptidases/*metabolism ; Molecular Sequence Data ; *Protein Biosynthesis ; *Protein Processing, Post-Translational ; Proteins/*metabolism ; RNA, Bacterial/genetics/*metabolism ; RNA, Messenger/genetics/metabolism ; RNA, Transfer/genetics/metabolism ; Ribosomes/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    The yeast cell cycle gene CDC34 encodes a ubiquitin-conjugating enzyme (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-09
    Description: Mutants in the gene CDC34 of the yeast Saccharomyces cerevisiae are defective in the transition from G1 to the S phase of the cell cycle. This gene was cloned and shown to encode a 295-residue protein that has substantial sequence similarity to the product of the yeast RAD6 gene. The RAD6 gene is required for a variety of cellular functions including DNA repair and was recently shown to encode a ubiquitin-conjugating enzyme. When produced in Escherichia coli, the CDC34 gene product catalyzed the covalent attachment of ubiquitin to histones H2A and H2B in vitro, demonstrating that the CDC34 protein is another distinct member of the family of ubiquitin-conjugating enzymes. The cell cycle function of CDC34 is thus likely to be mediated by the ubiquitin-conjugating activity of its product.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goebl, M G -- Yochem, J -- Jentsch, S -- McGrath, J P -- Varshavsky, A -- Byers, B -- GM18541/GM/NIGMS NIH HHS/ -- GM31530/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Sep 9;241(4871):1331-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2842867" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Cell Cycle ; Chromosome Mapping ; Cloning, Molecular ; *Genes, Fungal ; Molecular Sequence Data ; Protein Processing, Post-Translational ; Saccharomyces cerevisiae/*genetics ; Ubiquitins/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 6
    Electronic Resource
    Electronic Resource
    Ubiquitin-conjugating enzymes: novel regulators of eukaryotic cells
    Amsterdam : Elsevier
    Trends in Biochemical Sciences 15 (1990), S. 195-198 
    Details
    ISSN: 0968-0004
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0968-0004(90)90161-4
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    Paper (German National Licenses)
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  • 7
    Electronic Resource
    Electronic Resource
    Ubiquitin-dependent protein degradation: a cellular perspective
    Amsterdam : Elsevier
    Trends in Cell Biology 2 (1992), S. 98-103 
    Details
    ISSN: 0962-8924
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0962-8924(92)90013-D
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  • 8
    Electronic Resource
    Electronic Resource
    Genetic analysis of the ubiquitin system
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression 1089 (1991), S. 127-139 
    Details
    ISSN: 0167-4781
    Keywords: Cell cycle control ; Dna repair ; Proteolysis ; Ribosome assembly ; Stress response ; Ubiquitin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0167-4781(91)90001-3
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  • 9
    Electronic Resource
    Electronic Resource
    DNA methyltransferase genes of Bacillus subtilis phages: structural relatedness and gene expression
    Amsterdam : Elsevier
    Gene 35 (1985), S. 143-150 
    Details
    ISSN: 0378-1119
    Keywords: DNA modification ; Recombinant DNA ; evolution ; temperate bacteriophages SPR, φ3T, ρ11, SPβ, Z
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0378-1119(85)90166-0
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  • 10
    Electronic Resource
    Electronic Resource
    Restriction and modification in Bacillus subtilis: nucleotide sequence, functional organization and product of the DNA methyltransferase gene of bacteriophage SPR
    Amsterdam : Elsevier
    Gene 29 (1984), S. 51-61 
    Details
    ISSN: 0378-1119
    Keywords: DNA methylation ; Recombinant DNA ; heterologous gene expression ; translational and transcriptional starts
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0378-1119(84)90165-3
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