Accession Number : AD0785588

Title :   An Acidic, Alanine-rich 50 S Ribosomal Protein from 'Halobacterium cutirubrum': Amino Acid Sequence Homology with 'Escherichia coli' Proteins L7 and L12,

Corporate Author : NATIONAL RESEARCH COUNCIL OF CANADA OTTAWA (ONTARIO) DIV OF BIOLOGICAL SCIENCES

Personal Author(s) : Oda,G. ; Strom,A. R. ; Visentin,L. P. ; Yaguchi,M.

Report Date : 29 MAY 1974

Pagination or Media Count : 5

Abstract : The 50 S ribosomal subunits from H. cutirubrum contain an alanine-rich, acidic protein L20. Its high alanine content (over 25%), its acidity and its lack of histidine, cysteine and tryptophan residues make this protein a possible equivalent to the only sequenced 50 S ribosomal protein L7/L12 of E. coli. A large tryptic peptide (L20-T4), which belongs to the carboxyl-terminal half of the protein, has been isolated from H. cutirubrum L20. The amino-terminal regions of L20 and of peptide L20-T4 have been sequenced. The results indicate a high degree of homology of the first 30 residues of L20 with the central region of E. coli L7/L12 and the first 15 residues of L20-T4 with the carboxyl-terminal region of E. coli L7/L12.

Descriptors :   *Bacteria, *Pseudomonadaceae, *Ribosomes, *Proteins, Amino acids, Biosynthesis, Biochemistry, Canada

Subject Categories : Biochemistry
      Microbiology

Distribution Statement : APPROVED FOR PUBLIC RELEASE