| Autor: |
Vrontou E; Department of Biology, University of Crete, PO Box 1527, GR-71110 Iraklio, Crete, Greece., Karamanou S, Baud C, Sianidis G, Economou A |
| Jazyk: |
angličtina |
| Zdroj: |
The Journal of biological chemistry [J Biol Chem] 2004 May 21; Vol. 279 (21), pp. 22490-7. Date of Electronic Publication: 2004 Mar 07. |
| DOI: |
10.1074/jbc.M401008200 |
| Abstrakt: |
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 interdomain 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 couple 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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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