Procaryotic Ribosomal Proteins: N-Terminal Sequence Homologies and Structural Correspondence of 30 S Ribosomal Proteins from Escherichia coli and Bacillus stearothermophilus,
NATIONAL RESEARCH COUNCIL OF CANADA OTTAWA (ONTARIO) DIV OF BIOLOGICAL SCIENCES
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In attempting to evidence the evolution and the structure--function relationships of the ribosome in procaryotes the authors have undertaken a comparative amino acid sequence analysis of ribosomal proteins from Escherichia coli, and Bacillus stearothermophilus and Halobacterium cutirubrum, organisms which differ substantially in their physiological tolerances and taxonomic relationships. Previous structural studies have indicated a high degree of homology in some of the 30 S ribosomal proteins from E. coli and B. stearothermophilus. Reported in this paper is a summary of results on the study of the amino terminal regions of 19 ribosomal proteins E. coli strain Q13 and 21 from B. stearothermophilus strain 10.