Assembly of the translocase motor onto the preprotein-conducting channel.

Abstract:

:Bacterial protein secretion is catalysed by the SecYEG protein-conducting channel complexed with the SecA ATPase motor. To gain insight into the SecA-SecYEG interaction we used peptide arrays, thermodynamic quantification, mutagenesis and functional assays. Our data reveal that: (i) SecA binds with low affinity on several, peripheral, exposed SecYEG sites. This largely electrostatic association is modulated by temperature and nucleotides. (ii) Binding sites cluster in five major binding 'regions': three that are exclusively cytoplasmic and two that reach the periplasm. (iii) Both the N-terminal and c-terminal regions of SecA participate in binding interactions and share some sites. (iv) Several of these sites are essential for translocase catalysis. Our data provide residue-level dissection of the SecYEG-SecA interaction. Two models of assembly of SecA on dimeric SecYEG are discussed.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Karamanou S,Bariami V,Papanikou E,Kalodimos CG,Economou A

doi

10.1111/j.1365-2958.2008.06402.x

subject

Has Abstract

pub_date

2008-10-01 00:00:00

pages

311-22

issue

2

eissn

0950-382X

issn

1365-2958

pii

MMI6402

journal_volume

70

pub_type

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