Multiple forms of lysyl-transfer ribonucleic acid synthetase in Escherichia coli.

Abstract:

:Lysyl-transfer ribonucleic acid synthetase (EC 6.1.1.6) was identified as four polypeptide spots after two-dimensional polyacrylamide gel electrophoresis of whole-cell lysates of Escherichia coli. Identification was made by migration with partially purified enzyme preparations, by peptide map patterns, by mutant analysis, and by correlation of spot intensities with changes in enzyme levels under different growth conditions. Wild-type cells growing at 37 degrees C in glucose minimal medium displayed the enzyme predominantly as two spots (spots I and III). Growth at 46 degrees C, growth in the presence of alanine or glycyl-L-leucine, or growth of a strain with a mutational deficiency in S-adenosylmethionine synthetase (metK) greatly increased the synthesis of two other spots (spots II and IV). Polypeptides I and III, but not polypeptides II and IV, had altered isoelectric points in a lysyl-transfer ribonucleic acid synthetase mutant. These data suggest that multiple forms of lysyl-transfer ribonucleic acid synthetase exist in vivo and that they may be encoded by more than one gene.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Hirshfield IN,Bloch PL,Van Bogelen RA,Neidhardt FC

doi

10.1128/JB.146.1.345-351.1981

subject

Has Abstract

pub_date

1981-04-01 00:00:00

pages

345-51

issue

1

eissn

0021-9193

issn

1098-5530

journal_volume

146

pub_type

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