Membrane association of leucyl-tRNA synthetase during leucine starvation in Escherichia coli.

Abstract:

:The influence of leucine starvation on the subcellular location of leucyl-tRNA synthetase in Escherichia coli was examined in a leucine auxotrophic strain by sucrose density sedimentation analysis. Analysis of the subcellular distribution of leucyl-tRNA synthetase activity revealed that during unrestricted growth, the leucine synthetase enzyme activity was found to be localized in the soluble protein fraction of the gradient. However, during restricted growth on low levels of leucine, leucyl-tRNA synthetase activity was localized in the cytoplasmic membrane fraction of the gradient. The transition from soluble to membrane-association of the enzyme also occurred following inhibition of protein synthesis by treatment of cells with chloramphenicol. These results collectively suggest that leucyl-tRNA synthetase may be recruited to the cytoplasmic membrane in response to shortages of leucine or perturbation of protein synthesis.

authors

Williamson RM

doi

10.1006/bbrc.1993.1119

subject

Has Abstract

pub_date

1993-02-15 00:00:00

pages

794-800

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)71119-8

journal_volume

190

pub_type

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