Linked Life Data

7961469

Source:http://linkedlifedata.com/resource/pubmed/id/7961469

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pubmed-article:7961469pubmed:abstractTextThe translocation of ribosomes on mRNA is carried out by cellular machinery that has been extremely well conserved across the entire spectrum of living species. This process requires elongation factor G (EF-G, or EF-2 in archaebacteria and eukaryotes), which is a member of the GTPase superfamily. Using genetic techniques, we have identified a series of mutated alleles of fusA (the Escherichia coli gene that encodes EF-G) that were unable to support protein synthesis in vivo. These alleles encode proteins with point mutations at codons 495 (a variant with a Q-to-P change at codon 495 [Q495P]), 502 (G502D), and 563 (G563D) and a nonsense mutation at codon 608. Biochemical analyses demonstrated that EF-G Q495P, G502D, and delta 608-703 were not disrupted in guanine nucleotide binding but were deficient in ribosome-dependent GTP hydrolysis and guanine nucleotide-dependent ribosome association. We propose that all of these mutations are present in a domain that is essential for ribosome association and that GTP hydrolysis was deficient as a secondary consequence of impaired binding to 70S ribosomes.lld:pubmed
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pubmed-article:7961469pubmed:articleTitleCarboxyl-terminal amino acid residues in elongation factor G essential for ribosome association and translocation.lld:pubmed
pubmed-article:7961469pubmed:affiliationDepartment of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway 08854.lld:pubmed
pubmed-article:7961469pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7961469pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:7961469pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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