Structural homologies in alanine-rich acidic ribosomal proteins from procaryotes and eucaryotes

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DOIResolve DOI: http://doi.org/10.1139/o79-090
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TypeArticle
Journal titleCanadian Journal of Biochemistry
ISSN0829-8211
1208-6002
Volume57
Issue6
Pages719726; # of pages: 8
AbstractThe amino acid composition and amino-terminal sequence have been determined for the alanine-rich, acidic ribosomal 'A' protein (equivalent to Escherichia coli L7/L12) from three procaryotic cell types that live under extreme environmental conditions (Arthrobacter glacialis, Clostridium pasteurianum, and Bacillus stearothermophilus) as well as from wheat germ, a eucaryote source. These data are compared with previously published 'A' protein sequences from other procaryotes and eucaryotes. All the procaryotic 'A' proteins, with the exception of the very acidic 'A' protein from Halobacterium cutirubrum, show similar charge, size, and amino acid composition, as well as an extensive sequence homology in the N-terminal region. Some differences are observed between gram-negative and gram-positive bacteria. The 'A' proteins from eucaryotes contain two tyrosine molecules, an amino acid absent in procaryotic 'A' proteins, as well as a reduced number of valine residues and an increased amount of aspartic acid. The N-terminal sequence of wheat germ 'A' protein shows considerable homology with other eucaryotic 'A' proteins and also with H. cutirubrum. It also shows some sequence homology with E. coli 'A' proteins.
Publication date
PublisherNRC Research Press
LanguageEnglish
AffiliationNational Research Council Canada
NoteDr. Visentin and Yaguchi were affiliated with the National Research Council of Canada, Division of Biological Sciences when they authored this article.
Peer reviewedYes
NRC numberVISENTIN1979
NPARC number9381042
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Record identifiercd168eca-dffd-4161-83f3-dab4e5a75488
Record created2009-07-10
Record modified2017-07-25
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