PMID:15007058
| Citation |
Vrontou, E, Karamanou, S, Baud, C, Sianidis, G and Economou, A (2004) Global co-ordination of protein translocation by the SecA IRA1 switch. J. Biol. Chem. 279:22490-7 |
|---|---|
| Abstract |
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. |
| Links |
PubMed Online version:10.1074/jbc.M401008200 |
| Keywords |
Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/chemistry; Bacterial Proteins/metabolism; Catalysis; Catalytic Domain; DNA Mutational Analysis; Dimerization; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Hydrolysis; Kinetics; Ligands; Membrane Proteins/chemistry; Membrane Transport Proteins/metabolism; Models, Biological; Models, Molecular; Mutation; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Protein Transport; Spectrometry, Fluorescence; Surface Plasmon Resonance; Temperature |
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