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  • Alleles  (2)
  • Recombinant Fusion Proteins/metabolism
  • American Association for the Advancement of Science (AAAS)  (3)
  • American Physical Society (APS)
  • Public Library of Science
  • 2000-2004  (3)
  • 2001  (3)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (3)
  • American Physical Society (APS)
  • Public Library of Science
Years
  • 2000-2004  (3)
Year
  • 1
    Publication Date: 2001-11-03
    Description: Human immunodeficiency virus-1 (HIV-1) Vpr expression halts the proliferation of human cells at or near the G2 cell-cycle checkpoint. The transition from G2 to mitosis is normally controlled by changes in the state of phosphorylation and subcellular compartmentalization of key cell-cycle regulatory proteins. In studies of the intracellular trafficking of these regulators, we unexpectedly found that wild-type Vpr, but not Vpr mutants impaired for G2 arrest, induced transient, localized herniations in the nuclear envelope (NE). These herniations were associated with defects in the nuclear lamina. Intermittently, these herniations ruptured, resulting in the mixing of nuclear and cytoplasmic components. These Vpr-induced NE changes probably contribute to the observed cell-cycle arrest.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Noronha, C M -- Sherman, M P -- Lin, H W -- Cavrois, M V -- Moir, R D -- Goldman, R D -- Greene, W C -- KO8 AI01866/AI/NIAID NIH HHS/ -- P30 MH59037/MH/NIMH NIH HHS/ -- R01 AI145234/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2001 Nov 2;294(5544):1105-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gladstone Institute of Virology and Immunology, Department of Medicine, University of California, San Francisco, CA 94103, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11691994" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Cell Cycle Proteins/metabolism ; Cell Nucleus/*metabolism/virology ; Cyclin B/metabolism ; Cyclin B1 ; Cytoplasm/metabolism ; *G2 Phase ; Gene Products, vpr/genetics/*physiology ; HIV-1/*physiology ; HeLa Cells ; Humans ; *Lamin Type B ; Lamins ; Macrophages/virology ; Microscopy, Fluorescence ; Microscopy, Video ; Mitosis ; Mutation ; Nuclear Envelope/*metabolism/ultrastructure ; Nuclear Pore Complex Proteins/metabolism ; Nuclear Proteins/metabolism ; Protein-Tyrosine Kinases/metabolism ; Recombinant Fusion Proteins/metabolism ; Transfection ; Virus Integration ; cdc25 Phosphatases/metabolism ; vpr Gene Products, Human Immunodeficiency Virus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2001-04-21
    Description: Aminoacyl transfer RNA (tRNA) synthetases establish the rules of the genetic code by catalyzing the aminoacylation of tRNAs. For some synthetases, accuracy depends critically on an editing function at a site distinct from the aminoacylation site. Mutants of Escherichia coli that incorrectly charge tRNA(Val) with cysteine were selected after random mutagenesis of the whole chromosome. All mutations obtained were located in the editing site of valyl-tRNA synthetase. More than 20% of the valine in cellular proteins from such an editing mutant organism could be replaced with the noncanonical aminobutyrate, sterically similar to cysteine. Thus, the editing function may have played a central role in restricting the genetic code to 20 amino acids. Disabling this editing function offers a powerful approach for diversifying the chemical composition of proteins and for emulating evolutionary stages of ambiguous translation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doring, V -- Mootz, H D -- Nangle, L A -- Hendrickson, T L -- de Crecy-Lagard, V -- Schimmel, P -- Marliere, P -- GM23562/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Apr 20;292(5516):501-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Evologic SA, 4 rue Pierre Fontaine, 91000 Evry, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11313495" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Amino Acid Substitution ; Aminobutyrates/*metabolism ; Binding Sites ; Codon ; Cysteine/metabolism ; Escherichia coli/*genetics/growth & development/metabolism ; *Genetic Code ; Molecular Sequence Data ; Mutagenesis ; Phenotype ; *Protein Biosynthesis ; RNA, Bacterial/genetics/metabolism ; RNA, Transfer, Val/*metabolism ; Suppression, Genetic ; Threonine/metabolism ; Transfer RNA Aminoacylation ; Valine/metabolism ; Valine-tRNA Ligase/chemistry/genetics/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2001-09-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burghes, A H -- Vaessin, H E -- de La Chapelle, A -- New York, N.Y. -- Science. 2001 Sep 21;293(5538):2213-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biochemistry, Ohio State University, Columbus, OH 43210, USA. burghes.1@osu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11567125" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli/genetics ; Alleles ; Animals ; Bardet-Biedl Syndrome/*genetics ; Genes, APC ; Genes, Dominant ; Genes, Recessive ; Genetic Predisposition to Disease ; Genotype ; Humans ; *Multifactorial Inheritance ; Muscular Atrophy, Spinal/genetics ; Mutation ; Phenotype ; Proteins/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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