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Article

Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm.

Proceedings of the National Academy of Sciences of the United States of America - 23 Nov 1999

Bessette P H, Aslund F, Beckwith J, Georgiou G

Abstract excerpt

Under physiological conditions, the Escherichia coli cytoplasm is maintained in a reduced state that strongly disfavors the formation of stable disulfide bonds in proteins. However, mutants in which the reduction of both thioredoxins and glutathione is impaired (trxB gor mutants) accumulate oxidized, enzymatically active alkaline phosphatase in the cytoplasm. These mutants grow very poorly in the absence of an...

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Identifiers

PMID: 10570136
DOI: 10.1073/pnas.96.24.13703
PMCID: PMC24128

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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