期刊
EMBO JOURNAL
卷 23, 期 8, 页码 1868-1877出版社
WILEY
DOI: 10.1038/sj.emboj.7600172
关键词
methionine sulfoxide reductases; oxidative stress; pathogenicity; signal recognition particle
In proteins, methionine residues are primary targets for oxidation. Methionine oxidation is reversed by methionine sulfoxide reductases A and B, a class of highly conserved enzymes. Ffh protein, a component of the ubiquitous signal recognition particle, contains a methionine-rich domain, interacting with a small 4.5S RNA. In vitro analyses reported here show that: (i) oxidized Ffh is unable to bind 4.5S RNA, (ii) oxidized Ffh contains methionine sulfoxide residues, (iii) oxidized Ffh is a substrate for MsrA and MsrB enzymes; and (iv) MsrA/B repairing activities allow oxidized Ffh to recover 4.5S RNA-binding abilities. In vivo analyses reveal that: ( i) Ffh synthesized in the msrA msrB mutant contains methionine sulfoxide residues and is unstable, ( ii) msrA msrB mutant requires high levels of Ffh synthesis for growth and ( iii) msrA msrB mutation leads to defects in Ffh-dependent targeting of MalF. We conclude that MsrA and MsrB are required to repair Ffh oxidized by reactive oxygen species produced by aerobic metabolism, establishing an as-yet undescribed link between protein targeting and oxidation.
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