Abstract:
:The twin-arginine transport (Tat) system is a protein-targeting pathway of prokaryotes and chloroplasts. Most Escherichia coli Tat substrates are complex metalloenzymes that must be correctly folded and assembled before transport, and a preexport chaperone-mediated "proofreading" process is therefore in operation. The paradigm proofreading chaperone is TorD, which coordinates maturation and export of the key respiratory enzyme trimethylamine N-oxide reductase (TorA). It is demonstrated here that purified TorD binds tightly and with exquisite specificity to the TorA twin-arginine signal peptide in vitro. It is also reported that the TorD family constitutes a hitherto unexpected class of nucleotide-binding proteins. The affinity of TorD for GTP is enhanced by initial signal peptide binding, and it is proposed that GTP governs signal peptide binding-and-release cycles during Tat proofreading.
journal_name
Proc Natl Acad Sci U S Aauthors
Hatzixanthis K,Clarke TA,Oubrie A,Richardson DJ,Turner RJ,Sargent Fdoi
10.1073/pnas.0500737102keywords:
subject
Has Abstractpub_date
2005-06-14 00:00:00pages
8460-5issue
24eissn
0027-8424issn
1091-6490pii
0500737102journal_volume
102pub_type
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