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J. Biochem, 1980, Vol. 87, No. 4 1185-1201
© 1980 Japanese Biochemical Society

research-article

The Primary Structure of Bacillus subtilis Acidic Ribosomal Protein B-L9

Isolation and Characterization of Peptides and the Complete Amino Acid Sequence

Takuzi ITOH1 and Brigitte WITTMANN-LIEBOLD

Max-Planck-Institut für Molekulare Genetik Abteilung Wittmann D-1000 Berlin-Dahlem, Germany

The complete primary structure of Bacillus subtilis acidic protein B-L9, functionally equivalent to protein L7/L12 from E. coli has been determined. B-L9 is composed of 122 residues and has the amino acid composition: Asp3, Asn3, Thr4, Ser8, Glu22, Gln1, Pro3, Gly11, Ala21, Val14, Ile2, Leu12, Phe2, Lys13, and Arg1. The molecular weight of B-L9 is 12,633. The amino acid sequence was determined by a combination of automated Edman degradation of the intact protein in a modified Beckman sequenator, and micro dansyl-Edman degradation of the peptides obtained from digestions with trypsin, thermolysin, Staphylococcus aureus protease, chymotrypsin and pepsin. A comparison of protein B-L9 from B. subtilis with E-L12 from E. coli shows a relatively high degree of homology.

1 Present address: Department of Biochemistry and Biophysics, Research Institute of Nuclear Medicine and Biology, Hiroshima University, Hiroshima, Hiroshima 734.


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