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

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 Ds...

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Bibliografiske detaljer
Main Authors: Huber, Damon, Cha, Myoung-il, Debarbieux, Laurent, Planson, Anne-Gaëlle, Cruz, Nelly, López, Gary, Tasayco, María Luisa, Chaffotte, Alain, Beckwith, Jon
Format: Artigo
Sprog:Inglês
Udgivet: National Academy of Sciences 2005
Fag:
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC1323206/
https://ncbi.nlm.nih.gov/pubmed/16357193
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0509583102
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