ArticleFEBS letters2010
Comparing system-specific chaperone interactions with their Tat dependent redox enzyme substrates.
Article in FEBS letters, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- History of Maturation of Prokaryotic Molybdoenzymes-A Personal View.Molecules (Basel, Switzerland) · 2023Review
- Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.PloS one · 2021Article
- Same but different: Comparison of two system-specific molecular chaperones for the maturation of formate dehydrogenases.PloS one · 2018Article
- Characterization of a periplasmic nitrate reductase in complex with its biosynthetic chaperone.The FEBS journal · 2014Article
- Detrimental effect of the 6 His C-terminal tag on YedY enzymatic activity and influence of the TAT signal sequence on YedY synthesis.BMC biochemistry · 2013Article
- The hydrophobic region of the DmsA twin-arginine leader peptide determines specificity with chaperone DmsD.Biochemistry · 2013Article
- The hydrophobic core of twin-arginine signal sequences orchestrates specific binding to Tat-pathway related chaperones.PloS one · 2012Article
- Correct assembly of iron-sulfur cluster FS0 into Escherichia coli dimethyl sulfoxide reductase (DmsABC) is a prerequisite for molybdenum cofactor insertion.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Redox enzyme substrates of the twin-arginine translocation (Tat) system contain a RR-motif in their leader peptide and require the assistance of chaperones, redox enzyme maturation proteins (REMPs). Here various regions of the RR-containing oxidoreductase subunit (leader peptide, full preprotein with and without a leader cleavage site, mature protein) were assayed for interaction with their REMPs. All REMPs bound their preprotein substrates independent of the cleavage site. Some showed binding to either the leader or mature region, whereas in one case only the preprotein bound its REMP. The absence of Tat also influenced the amount of chaperone-substrate interaction.
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Registered trials
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