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  • Evolution
  • Saccharomyces cerevisiae
  • pharmacokinetics
  • American Association for the Advancement of Science (AAAS)  (4)
  • Peter Lang International Academic Publishing Group
  • Springer
  • Springer Nature
  • 2010-2014  (4)
Collection
Keywords
Publisher
Years
Year
  • 1
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    Molecular architecture of a eukaryotic translational initiation complex (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-11-10
    Description: The last step in eukaryotic translational initiation involves the joining of the large and small subunits of the ribosome, with initiator transfer RNA (Met-tRNA(i)(Met)) positioned over the start codon of messenger RNA in the P site. This step is catalyzed by initiation factor eIF5B. We used recent advances in cryo-electron microscopy (cryo-EM) to determine a structure of the eIF5B initiation complex to 6.6 angstrom resolution from 〈3% of the population, comprising just 5143 particles. The structure reveals conformational changes in eIF5B, initiator tRNA, and the ribosome that provide insights into the role of eIF5B in translational initiation. The relatively high resolution obtained from such a small fraction of a heterogeneous sample suggests a general approach for characterizing the structure of other dynamic or transient biological complexes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3836175/" 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/PMC3836175/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fernandez, Israel S -- Bai, Xiao-Chen -- Hussain, Tanweer -- Kelley, Ann C -- Lorsch, Jon R -- Ramakrishnan, V -- Scheres, Sjors H W -- 096570/Wellcome Trust/United Kingdom -- MC_U105184332/Medical Research Council/United Kingdom -- MC_UP_A025_1013/Medical Research Council/United Kingdom -- WT096570/Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2013 Nov 15;342(6160):1240585. doi: 10.1126/science.1240585. Epub 2013 Nov 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge CB2 0QH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24200810" target="_blank"〉PubMed〈/a〉
    Keywords: Analytic Sample Preparation Methods ; Cryoelectron Microscopy/methods ; Eukaryotic Initiation Factors/*chemistry ; Humans ; *Peptide Chain Initiation, Translational ; Protein Conformation ; RNA, Transfer, Met/chemistry ; Ribosomes/*chemistry ; Saccharomyces cerevisiae
    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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  • 2
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    CTD tyrosine phosphorylation impairs termination factor recruitment to RNA polymerase II (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-30
    Description: In different phases of the transcription cycle, RNA polymerase (Pol) II recruits various factors via its C-terminal domain (CTD), which consists of conserved heptapeptide repeats with the sequence Tyr(1)-Ser(2)-Pro(3)-Thr(4)-Ser(5)-Pro(6)-Ser(7). We show that the CTD of transcribing yeast Pol II is phosphorylated at Tyr(1), in addition to Ser(2), Thr(4), Ser(5), and Ser(7). Tyr(1) phosphorylation stimulates binding of elongation factor Spt6 and impairs recruitment of termination factors Nrd1, Pcf11, and Rtt103. Tyr(1) phosphorylation levels rise downstream of the transcription start site and decrease before the polyadenylation site, largely excluding termination factors from gene bodies. These results show that CTD modifications trigger and block factor recruitment and lead to an extended CTD code that explains transcription cycle coordination on the basis of differential phosphorylation of Tyr(1), Ser(2), and Ser(5).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mayer, Andreas -- Heidemann, Martin -- Lidschreiber, Michael -- Schreieck, Amelie -- Sun, Mai -- Hintermair, Corinna -- Kremmer, Elisabeth -- Eick, Dirk -- Cramer, Patrick -- New York, N.Y. -- Science. 2012 Jun 29;336(6089):1723-5. doi: 10.1126/science.1219651.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gene Center and Department of Biochemistry, Center for Integrated Protein Science Munich, Ludwig-Maximilians-Universitat Munchen, Feodor-Lynen-Strasse 25, 81377 Munich, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22745433" target="_blank"〉PubMed〈/a〉
    Keywords: Catalytic Domain ; Chromatin Immunoprecipitation ; HeLa Cells ; Humans ; Peptide Termination Factors/metabolism ; Phosphorylation ; Protein Kinases/metabolism ; RNA Polymerase II/*metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins/metabolism ; Transcriptional Elongation Factors/metabolism ; Tyrosine/*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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  • 3
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    Positive supercoiling of mitotic DNA drives decatenation by topoisomerase II in eukaryotes (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-03-12
    Description: DNA topoisomerase II completely removes DNA intertwining, or catenation, between sister chromatids before they are segregated during cell division. How this occurs throughout the genome is poorly understood. We demonstrate that in yeast, centromeric plasmids undergo a dramatic change in their topology as the cells pass through mitosis. This change is characterized by positive supercoiling of the DNA and requires mitotic spindles and the condensin factor Smc2. When mitotic positive supercoiling occurs on decatenated DNA, it is rapidly relaxed by topoisomerase II. However, when positive supercoiling takes place in catenated plasmid, topoisomerase II activity is directed toward decatenation of the molecules before relaxation. Thus, a topological change on DNA drives topoisomerase II to decatenate molecules during mitosis, potentially driving the full decatenation of the genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baxter, J -- Sen, N -- Martinez, V Lopez -- De Carandini, M E Monturus -- Schvartzman, J B -- Diffley, J F X -- Aragon, L -- MC_U120074328/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- Cancer Research UK/United Kingdom -- New York, N.Y. -- Science. 2011 Mar 11;331(6022):1328-32. doi: 10.1126/science.1201538.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council (MRC) Clinical Sciences Centre, Imperial College London, Hammersmith Hospital, London, UK. Jon.Baxter@sussex.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21393545" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Cycle ; Chromosome Segregation ; DNA Replication ; DNA Topoisomerases, Type II/*metabolism ; DNA, Catenated/*chemistry/metabolism ; DNA, Fungal/*chemistry/metabolism ; DNA, Superhelical/*chemistry/metabolism ; Dimerization ; *Mitosis ; Nucleic Acid Conformation ; Plasmids ; Saccharomyces cerevisiae ; Spindle Apparatus/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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  • 4
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    Adaptation and evolutionary rescue in metapopulations experiencing environmental deterioration (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-06-11
    Description: It is not known whether evolution will usually be rapid enough to allow a species to adapt and persist in a deteriorating environment. We tracked the eco-evolutionary dynamics of metapopulations with a laboratory model system of yeast exposed to salt stress. Metapopulations experienced environmental deterioration at three different rates and their component populations were either unconnected or connected by local dispersal or by global dispersal. We found that adaptation was favored by gradual deterioration and local dispersal. After further abrupt deterioration, the frequency of evolutionary rescue depended on both the prior rate of deterioration and the rate of dispersal. Adaptation was surprisingly frequent and rapid in small peripheral populations. Thus, evolutionary dynamics affect both the persistence and the range of a species after environmental deterioration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bell, Graham -- Gonzalez, Andrew -- New York, N.Y. -- Science. 2011 Jun 10;332(6035):1327-30. doi: 10.1126/science.1203105.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, McGill University, 1205 ave Docteur Penfield, Montreal, Quebec H3A 1B1, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21659606" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptation, Physiological ; *Biological Evolution ; Directed Molecular Evolution ; *Environment ; Models, Biological ; Saccharomyces cerevisiae
    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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