Abstract:
:The twin-arginine translocation (Tat) system serves to translocate folded and often cofactor-containing proteins across biological membranes. The mechanistic limits of the Tat system can be explored by addressing the transport of specifically designed Tat substrates. It thus could be recently shown that unstructured proteins are also accepted by the Tat system, but only if they are polar on their surface. Using the iron-sulfur cofactor-containing model Tat-substrate high potential iron-sulfur protein (HiPIP), we now demonstrate that the bacterial Tat system can translocate small globular proteins even when a long unstructured linker peptide of 110 residues is sandwiched between the signal peptide and the N-terminus of the mature domain. The iron-sulfur cofactor was fully assembled in the transported protein, which demonstrates that HiPIP was folded during translocation. Linker lengths of 148 and 205 residues almost blocked or completely abolished Tat transport, respectively. The tolerance for long unfolded linker peptides challenges our current understanding of the Tat mechanism.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Lindenstrauss U,Brüser Tdoi
10.1111/j.1574-6968.2009.01600.xsubject
Has Abstractpub_date
2009-06-01 00:00:00pages
135-40issue
1eissn
0378-1097issn
1574-6968pii
FML1600journal_volume
295pub_type
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