GroE is vital for cell-wall synthesis

Neil McLennan and Millicent Masters ()
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Neil McLennan: Institute of Cell and Molecular Biology, Edinburgh University
Millicent Masters: Institute of Cell and Molecular Biology, Edinburgh University

Nature, 1998, vol. 392, issue 6672, 139-139

Abstract: Abstract Chaperone proteins help other proteins to fold. GroEL, the Escherichia coli form of the ubiquitous Cpn60 chaperonins, has a multimeric barrel-shaped structure with a central cavity, within which almost any protein can fold in vitro1. But what does GroE (GroEL plus its co-chaperone GroES) fold in the cell? Why is it needed for cell survival2? We report here the first definite identification of an essential, GroE-dependent E. coli protein, dihydropicolinate synthase (DapA), without which cell-wall synthesis fails.

Date: 1998
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DOI: 10.1038/32317

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