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GroE is vital for cell-wall synthesis

Nature volume 392, page 139 (1998)Cite this article

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.

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Figure 1: Depletion of GroE in E. coli.
Figure 2: DapA loss in GroE-depleted cells.

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Authors and Affiliations

  1. Institute of Cell and Molecular Biology, Edinburgh University, Kings Buildings, Mayfield Road, Edinburgh, EH9 3JR, UK

    Neil McLennan & Millicent Masters

Authors
  1. Neil McLennan
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  2. Millicent Masters
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McLennan, N., Masters, M. GroE is vital for cell-wall synthesis. Nature 392, 139 (1998). https://doi.org/10.1038/32317

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