Cysteine homeostasis under inhibition of protein synthesis in Escherichia coli cells.

Abstract:

:Increased intracellular cysteine poses a potential danger to cells due to the high ability of cysteine to reduce free iron and promote the Fenton reaction. Here, we studied ways to maintain cysteine homeostasis in E. coli cells while inhibiting protein synthesis with valine or chloramphenicol. When growing wild-type bacteria on minimal medium with sulfate, an excess of cysteine resulting from the inhibition of protein synthesis is mainly incorporated into glutathione (up to 90%), which, therefore, can be considered as cysteine buffer. The share of hydrogen sulfide, which is the product of cysteine degradation by cysteine synthase B (CysM), does not exceed 1-3%, the rest falls on free cysteine, exported from cells. As a result, intracellular free cysteine is maintained at a low level (about 0.1 mM). The lack of glutathione in the gshA mutant increases H2S production and excretion of cysteine and leads to a threefold increase in the level of intracellular cysteine in response to valine and chloramphenicol. The relA mutants, exposed to valine, produce more H2S, dramatically accelerate the export of glutathione and accumulate more cysteine in the cytoplasm than their parent, which indicates that the regulatory nucleotide (p)ppGpp is involved in maintaining cysteine homeostasis. Disruption of cysteine homeostasis in gshA and relA mutants increases their sensitivity to peroxide stress.

journal_name

Amino Acids

journal_title

Amino acids

authors

Smirnova GV,Tyulenev AV,Bezmaternykh KV,Muzyka NG,Ushakov VY,Oktyabrsky ON

doi

10.1007/s00726-019-02795-2

subject

Has Abstract

pub_date

2019-11-01 00:00:00

pages

1577-1592

issue

10-12

eissn

0939-4451

issn

1438-2199

pii

10.1007/s00726-019-02795-2

journal_volume

51

pub_type

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