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  • Articles  (4)
  • Cell & Developmental Biology
  • Saccharomyces cerevisiae
  • 1990-1994  (4)
  • 1945-1949
  • 1940-1944
  • 1925-1929
  • 1920-1924
  • 1900-1904
  • 1994  (4)
  • 1929
  • Science. 264(5164): 1427-33.  (1)
  • Science. 265(5172): 674-6.  (1)
  • Science. 265(5176): 1241-3.  (1)
  • Science. 265(5179): 1716-9.  (1)
  • 25
  • Biology  (4)
  • Process Engineering, Biotechnology, Nutrition Technology
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  • Articles  (4)
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  • 1990-1994  (4)
  • 1945-1949
  • 1940-1944
  • 1925-1929
  • 1920-1924
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  • 1
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    Structure of the allosteric regulatory enzyme of purine biosynthesis (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-03
    Description: Multi-wavelength anomalous diffraction (MAD) has been used to determine the structure of the regulatory enzyme of de novo synthesis of purine nucleotides, glutamine 5-phosphoribosyl-1-pyrophosphate (PRPP) amidotransferase, from Bacillus subtilis. This allosteric enzyme, a 200-kilodalton tetramer, is subject to end product regulation by purine nucleotides. The metalloenzyme from B. subtilis is a paradigm for the higher eukaryotic enzymes, which have been refractory to isolation in stable form. The two folding domains of the polypeptide are correlated with functional domains for glutamine binding and for transfer of ammonia to the substrate PRPP. Eight molecules of the feedback inhibitor adenosine monophosphate (AMP) are bound to the tetrameric enzyme in two types of binding sites: the PRPP catalytic site of each subunit and an unusual regulatory site that is immediately adjacent to each active site but is between subunits. An oxygen-sensitive [4Fe-4S] cluster in each subunit is proposed to regulate protein turnover in vivo and is distant from the catalytic site. Oxygen sensitivity of the cluster is diminished by AMP, which blocks a channel through the protein to the cluster. The structure is representative of both glutamine amidotransferases and phosphoribosyltransferases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, J L -- Zaluzec, E J -- Wery, J P -- Niu, L -- Switzer, R L -- Zalkin, H -- Satow, Y -- DK-42303/DK/NIDDK NIH HHS/ -- GM-24658/GM/NIGMS NIH HHS/ -- R37 DK042303/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 3;264(5164):1427-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Purdue University, West Lafayette, IN 47907.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8197456" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Monophosphate/metabolism ; Allosteric Regulation ; Amidophosphoribosyltransferase/*chemistry/metabolism ; Amino Acid Sequence ; Animals ; Bacillus subtilis/*enzymology ; Binding Sites ; Computer Graphics ; Crystallography, X-Ray ; Humans ; Models, Molecular ; Molecular Sequence Data ; Oxygen/pharmacology ; Protein Folding ; Protein Structure, Secondary ; 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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    Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-29
    Description: Transforming growth factor-beta (TGF-beta) family members bind to receptors that consist of heteromeric serine-threonine kinase subunits (type I and type II). In a yeast genetic screen, the immunophilin FKBP-12, a target of the macrolides FK506 and rapamycin, interacted with the type I receptor for TGF-beta and with other type I receptors. Deletion, point mutation, and co-immunoprecipitation studies further demonstrated the specificity of the interaction. Excess FK506 competed with type I receptors for binding to FKBP-12, which suggests that these receptors share or overlap the macrolide binding site on FKBP-12, and therefore they may represent its natural ligand. The specific interaction between the type I receptors and FKBP-12 suggests that FKBP-12 may play a role in type I receptor-mediated signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, T -- Donahoe, P K -- Zervos, A S -- CA17393/CA/NCI NIH HHS/ -- NICHD P-30 HD28138/HD/NICHD NIH HHS/ -- NICHD P-32 HD07396/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1994 Jul 29;265(5172):674-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cutaneous Biology Research Center, Massachusetts General Hospital, Boston, MA 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7518616" target="_blank"〉PubMed〈/a〉
    Keywords: Binding, Competitive ; Carrier Proteins/*metabolism ; Heat-Shock Proteins/*metabolism ; Point Mutation ; Precipitin Tests ; Protein-Serine-Threonine Kinases/metabolism ; Receptors, Transforming Growth Factor beta/*metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae ; Tacrolimus/metabolism ; Tacrolimus Binding Proteins
    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
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    Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-16
    Description: Intracellular signaling from receptor tyrosine kinases in mammalian cells results in activation of a signal cascade that includes the guanine nucleotide-binding protein Ras and the protein kinases Raf, MEK [mitogen-activated protein kinase (MAPK) or extracellular signal-regulated kinase (ERK) kinase], and MAPK. MAPK activation that is dependent on the coupling of Ras and Raf was reconstituted in yeast. Yeast genes were isolated that, when overexpressed, enhanced the function of Raf. One of them is identical to BMH1, which encodes a protein similar to members of the mammalian 14-3-3 family. Bacterially synthesized mammalian 14-3-3 protein stimulated the activity of Raf prepared from yeast cells expressing c-Raf-1. Thus, the 14-3-3 protein may participate in or be required for activation of Raf.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Irie, K -- Gotoh, Y -- Yashar, B M -- Errede, B -- Nishida, E -- Matsumoto, K -- New York, N.Y. -- Science. 1994 Sep 16;265(5179):1716-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Faculty of Science, Nagoya University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8085159" target="_blank"〉PubMed〈/a〉
    Keywords: 14-3-3 Proteins ; Amino Acid Sequence ; Enzyme Activation ; Fungal Proteins/genetics/*metabolism ; GTP-Binding Proteins/genetics/metabolism ; Molecular Sequence Data ; Nerve Tissue Proteins/genetics/*metabolism ; Protein-Serine-Threonine Kinases/chemistry/*metabolism ; Proto-Oncogene Proteins/chemistry/*metabolism ; Proto-Oncogene Proteins c-raf ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae ; *Saccharomyces cerevisiae Proteins ; *Tyrosine 3-Monooxygenase ; *ras Proteins
    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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  • 4
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    Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-26
    Description: The RAD51 gene of Saccharomyces cerevisiae is required for genetic recombination and DNA double-strand break repair. Here it is demonstrated that RAD51 protein pairs circular viral single-stranded DNA from phi X 174 or M13 with its respective homologous linear double-stranded form. The product of synapsis between these DNA partners is further processed by RAD51 to yield nicked circular duplex DNA, which indicates that RAD51 can catalyze strand exchange. The pairing and strand exchange reaction requires adenosine triphosphate, a result consistent with the presence of a DNA-dependent adenosine triphosphatase activity in RAD51 protein. Thus, RAD51 is a eukaryotic recombination protein that can catalyze the strand exchange reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sung, P -- New York, N.Y. -- Science. 1994 Aug 26;265(5176):1241-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sealy Center for Molecular Science, University of Texas Medical Branch at Galveston 77555-1061.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8066464" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/*metabolism ; Bacteriophage M13 ; Bacteriophage phi X 174 ; Base Composition ; Catalysis ; DNA, Circular/*metabolism ; DNA, Single-Stranded/*metabolism ; DNA, Viral/*metabolism ; DNA-Binding Proteins/*metabolism ; Fungal Proteins/*metabolism ; Rad51 Recombinase ; Replication Protein A ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins
    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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