Journal
FASEB JOURNAL
Volume 28, Issue 5, Pages 2146-2157Publisher
FEDERATION AMER SOC EXP BIOL
DOI: 10.1096/fj.13-241430
Keywords
Paracoccus denitrificans; regulation
Categories
Funding
- Programa de Apoyo a Proyectos de Investigacion e Innovacion Tecnologica (PAPIIT)-Direccion General Asuntos del Personal Academico (DGAPA
- UNAM) [IN213809, IN211012]
- Consejo Nacional de Ciencia y Tecnologia (CONACyT) grant [CB-2011-01-167622]
- CONACyT grant [47310013, 105532]
- PAPIIT-DGAPA (UNAM) grant [IN215912]
- CONACyT Ph.D. Fellowship [299475]
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The subunit is a novel natural inhibitor of the -proteobacterial F1FO-ATPase described originally in Paracoccus denitrificans. To characterize the mechanism by which this subunit inhibits the F1FO nanomotor, the subunit of Paracoccus denitrificans (Pd-) was analyzed by the combination of kinetic, biochemical, bioinformatic, proteomic, and structural approaches. The subunit causes full inhibition of the sulfite-activated PdF1-ATPase with an apparent IC50 of 270 nM by a mechanism independent of the epsilon subunit. The inhibitory region of the subunit resides in the first 14 N-terminal residues of the protein, which protrude from the 4--helix bundle structure of the isolated subunit, as resolved by NMR. Cross-linking experiments show that the subunit interacts with rotor () and stator (, ) subunits of the F-1-ATPase, indicating that the subunit hinders rotation of the central stalk. In addition, a putatively regulatory nucleotide-binding site was found in the subunit by isothermal titration calorimetry. Together, the data show that the subunit controls the rotation of F1FO-ATPase by a mechanism reminiscent of, but different from, those described for mitochondrial IF1 and bacterial epsilon subunits where the 4--helix bundle of seems to work as an anchoring domain that orients the N-terminal inhibitory domain to hinder rotation of the central stalk.Zarco-Zavala, M., Morales-Rios, E., Mendoza-Hernandez, G., Ramirez-Silva, L., Perez-Hernandez, G., Garcia-Trejo, J. J. The subunit of the F1FO-ATP synthase of -proteobacteria controls rotation of the nanomotor with a different structure.
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