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  • 1
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    A biochemical genomics approach for identifying genes by the activity of their products (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-11-05
    Description: For the identification of yeast genes specifying biochemical activities, a genomic strategy that is rapid, sensitive, and widely applicable was developed with an array of 6144 individual yeast strains, each containing a different yeast open reading frame (ORF) fused to glutathione S-transferase (GST). For the identification of ORF-associated activities, strains were grown in defined pools, and GST-ORFs were purified. Then, pools were assayed for activities, and active pools were deconvoluted to identify the source strains. Three previously unknown ORF-associated activities were identified with this strategy: a cyclic phosphodiesterase that acts on adenosine diphosphate-ribose 1"-2" cyclic phosphate (Appr〉p), an Appr-1"-p-processing activity, and a cytochrome c methyltransferase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martzen, M R -- McCraith, S M -- Spinelli, S L -- Torres, F M -- Fields, S -- Grayhack, E J -- Phizicky, E M -- GM52347/GM/NIGMS NIH HHS/ -- P41 RR11823/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1999 Nov 5;286(5442):1153-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of Rochester School of Medicine, Rochester, NY 14642, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10550052" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate Ribose/analogs & derivatives/metabolism ; Fungal Proteins/*genetics/metabolism ; *Genes, Fungal ; *Genetic Techniques ; Glutathione Transferase/genetics ; Histone-Lysine N-Methyltransferase/genetics/isolation & purification/metabolism ; *Open Reading Frames ; Phosphoric Diester Hydrolases/genetics/isolation & purification/metabolism ; Recombinant Fusion Proteins/isolation & purification ; Saccharomyces cerevisiae/*genetics ; Sensitivity and Specificity
    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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    An NAD derivative produced during transfer RNA splicing: ADP-ribose 1"-2" cyclic phosphate (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-09
    Description: Transfer RNA (tRNA) splicing is essential in Saccharomyces cerevisiae as well as in humans, and many of its features are the same in both. In yeast, the final step of this process is removal of the 2' phosphate generated at the splice junction during ligation. A nicotinamide adenine dinucleotide (NAD)-dependent phosphotransferase catalyzes removal of the 2' phosphate and produces a small molecule. It is shown here that this small molecule is an NAD derivative: adenosine diphosphate (ADP)-ribose 1"-2" cyclic phosphate. Evidence is also presented that this molecule is produced in Xenopus laevis oocytes as a result of dephosphorylation of ligated tRNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Culver, G M -- McCraith, S M -- Zillmann, M -- Kierzek, R -- Michaud, N -- LaReau, R D -- Turner, D H -- Phizicky, E M -- DE07202-02/DE/NIDCR NIH HHS/ -- GM 22939/GM/NIGMS NIH HHS/ -- GM 25349/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jul 9;261(5118):206-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Rochester School of Medicine and Dentistry, NY 14642.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8392224" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate Ribose/*analogs & derivatives/chemistry/metabolism ; Animals ; Cyclic ADP-Ribose ; Endoribonucleases/metabolism ; NAD/chemistry/metabolism ; Oocytes/metabolism ; Phosphates/metabolism ; Phosphorylation ; Phosphotransferases/metabolism ; *RNA Splicing ; RNA, Fungal/*metabolism ; RNA, Transfer/*metabolism ; Saccharomyces cerevisiae/*genetics ; Xenopus
    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)
    Location Call Number Expected Availability
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    PAPER CURRENT
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