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• W1989121941 abstract "A comparative genomic analysis predicted that many members of the under-characterized COG0523 subfamily of putative P-loop GTPases function in metal metabolism. In this work we focused on the uncharacterized Escherichia coli protein YeiR by studying both the physiology of a yeiR mutant and the in vitro biochemical properties of YeiR expressed as a fusion with the maltose-binding protein (YeiR-MBP). Our results demonstrate that deletion of yeiR increases the sensitivity of E. coli to EDTA or cadmium, and this phenotype is linked to zinc depletion. In vitro, the tagged protein binds several Zn(2+) ions with nanomolar affinity and oligomerizes in the presence of metal. The GTPase activity of YeiR is similar to that measured for other members of the group, but GTP hydrolysis is enhanced by Zn(2+) binding. These results support the predicted connection between the COG0523 P-loop GTPases and roles in metal homeostasis." @default.
• W1989121941 created "2016-06-24" @default.
• W1989121941 creator A5013938980 @default.
• W1989121941 creator A5016943002 @default.
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• W1989121941 creator A5049226429 @default.
• W1989121941 date "2012-01-01" @default.
• W1989121941 modified "2023-10-16" @default.
• W1989121941 title "YeiR: a metal-binding GTPase from Escherichia coli involved in metal homeostasis" @default.
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• W1989121941 doi "https://doi.org/10.1039/c2mt20012k" @default.
• W1989121941 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3574555" @default.
• W1989121941 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22511334" @default.
• W1989121941 hasPublicationYear "2012" @default.
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