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A more recent version of this article appeared on May 21, 2004 Originally published In Press as doi:10.1074/jbc.M401008200 on March 7, 2004
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Papers In Press, published online ahead of print March 9, 2004
J. Biol. Chem, 10.1074/jbc.M401008200
Submitted on January 29, 2004
Revised on March 4, 2004
Accepted on March 7, 2004

Global co-ordination of protein translocation by the SecA IRA1 switch

Eleftheria Vrontou, Spyridoula Karamanou, Catherine Baud, Giorgos Sianidis, and Anastassios Economou

IMBB & Department of Biology, U.Crete, Iraklio, Crete, GREECE

Corresponding Author: aeconomo{at}imbb.forth.gr

SecA, the dimeric ATPase subunit of protein translocase, contains a DEAD helicase catalytic core that binds to a regulatory C-terminal domain. We now demonstrate that IRA1, a conserved helix-loop-helix structure in the C-domain, controls C-domain conformation through direct inter-domain contacts. C-domain conformational changes are transmitted to the DEAD motor and alter its conformation. These interactions establish DEAD motor/C-domain conformational cross-talk that requires a functional IRA1. IRA1-controlled binding/release cycles of the C-domain to the DEAD motor, couples this cross-talk to protein translocation chemistries, i.e. DEAD motor affinities for ligands (nucleotides, preprotein signal peptides and SecYEG, the integral membrane component of translocase) and ATP turnover. IRA1-mediated global co-ordination of SecA catalysis is essential for protein translocation.


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