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Article

A selection for mutants that interfere with folding of Escherichia coli thioredoxin-1 in vivo.

Proceedings of the National Academy of Sciences of the United States of America - 27 Dec 2005

Huber Damon, Cha Myoung-Il, Debarbieux Laurent, Planson Anne-Gaëlle, Cruz Nelly, López Gary, Tasayco María Luisa, Chaffotte Alain, Beckwith Jon

Abstract excerpt

Escherichia coli thioredoxin is normally a cytoplasmic protein involved in the reduction of disulfide bonds. However, thioredoxin can be translocated to the periplasm when it is attached to a cotranslational signal sequence. When exported to the periplasm, it can partially replace the activity of DsbA in promoting the formation of disulfide bonds. In contrast, when thioredoxin is fused to a posttranslational...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 16357193
DOI: 10.1073/pnas.0509583102
PMCID: PMC1323206

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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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