Effect of the ATPase inhibitor protein IF{sub 1} on H{sup +} translocation in the mitochondrial ATP synthase complex
Abstract
The H{sup +} F{sub o}F{sub 1}-ATP synthase complex of coupling membranes converts the proton-motive force into rotatory mechanical energy to drive ATP synthesis. The F{sub 1} moiety of the complex protrudes at the inner side of the membrane, the F{sub o} sector spans the membrane reaching the outer side. The IF{sub 1} component of the mitochondrial complex is a basic 10 kDa protein, which inhibits the F{sub o}F{sub 1}-ATP hydrolase activity. The mitochondrial matrix pH is the critical factor for the inhibitory binding of the central segment of IF{sub 1} (residue 42-58) to the F{sub 1}-{alpha}/{beta} subunits. We have analyzed the effect of native purified IF{sub 1} the IF{sub 1}-(42-58) synthetic peptide and its mutants on proton conduction, driven by ATP hydrolysis or by [K{sup +}] gradients, in bovine heart inside-out submitochondrial particles and in liposome-reconstituted F{sub o}F{sub 1} complex. The results show that IF{sub 1}, and in particular its central 42-58 segment, displays different inhibitory affinity for proton conduction from the F{sub 1} to the F{sub o} side and in the opposite direction. Cross-linking of IF{sub 1} to F{sub 1}-{alpha}/{beta} subunits inhibits the ATP-driven H{sup +} translocation but enhances H{sup +} conduction in the reverse direction. These observation aremore »
- Authors:
-
- Dept. of Medical Biochemistry, Biology and Physics, University of Bari (Italy)
- Publication Date:
- OSTI Identifier:
- 22199720
- Resource Type:
- Journal Article
- Journal Name:
- Biochemical and Biophysical Research Communications
- Additional Journal Information:
- Journal Volume: 384; Journal Issue: 1; Other Information: Copyright (c) 2009 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 60 APPLIED LIFE SCIENCES; ATP; CATTLE; CROSS-LINKING; HEART; HYDROLYSIS; MEMBRANES; MUTANTS; PEPTIDES; PH VALUE; POTASSIUM IONS; PROTONS; TRANSLOCATION
Citation Formats
Zanotti, Franco, Inst. of Biomembranes and Bioenergetics, CNR, Bari, Gnoni, Antonio, Mangiullo, Roberto, Papa, Sergio, and Inst. of Biomembranes and Bioenergetics, CNR, Bari. Effect of the ATPase inhibitor protein IF{sub 1} on H{sup +} translocation in the mitochondrial ATP synthase complex. United States: N. p., 2009.
Web. doi:10.1016/J.BBRC.2009.04.046.
Zanotti, Franco, Inst. of Biomembranes and Bioenergetics, CNR, Bari, Gnoni, Antonio, Mangiullo, Roberto, Papa, Sergio, & Inst. of Biomembranes and Bioenergetics, CNR, Bari. Effect of the ATPase inhibitor protein IF{sub 1} on H{sup +} translocation in the mitochondrial ATP synthase complex. United States. https://doi.org/10.1016/J.BBRC.2009.04.046
Zanotti, Franco, Inst. of Biomembranes and Bioenergetics, CNR, Bari, Gnoni, Antonio, Mangiullo, Roberto, Papa, Sergio, and Inst. of Biomembranes and Bioenergetics, CNR, Bari. 2009.
"Effect of the ATPase inhibitor protein IF{sub 1} on H{sup +} translocation in the mitochondrial ATP synthase complex". United States. https://doi.org/10.1016/J.BBRC.2009.04.046.
@article{osti_22199720,
title = {Effect of the ATPase inhibitor protein IF{sub 1} on H{sup +} translocation in the mitochondrial ATP synthase complex},
author = {Zanotti, Franco and Inst. of Biomembranes and Bioenergetics, CNR, Bari and Gnoni, Antonio and Mangiullo, Roberto and Papa, Sergio and Inst. of Biomembranes and Bioenergetics, CNR, Bari},
abstractNote = {The H{sup +} F{sub o}F{sub 1}-ATP synthase complex of coupling membranes converts the proton-motive force into rotatory mechanical energy to drive ATP synthesis. The F{sub 1} moiety of the complex protrudes at the inner side of the membrane, the F{sub o} sector spans the membrane reaching the outer side. The IF{sub 1} component of the mitochondrial complex is a basic 10 kDa protein, which inhibits the F{sub o}F{sub 1}-ATP hydrolase activity. The mitochondrial matrix pH is the critical factor for the inhibitory binding of the central segment of IF{sub 1} (residue 42-58) to the F{sub 1}-{alpha}/{beta} subunits. We have analyzed the effect of native purified IF{sub 1} the IF{sub 1}-(42-58) synthetic peptide and its mutants on proton conduction, driven by ATP hydrolysis or by [K{sup +}] gradients, in bovine heart inside-out submitochondrial particles and in liposome-reconstituted F{sub o}F{sub 1} complex. The results show that IF{sub 1}, and in particular its central 42-58 segment, displays different inhibitory affinity for proton conduction from the F{sub 1} to the F{sub o} side and in the opposite direction. Cross-linking of IF{sub 1} to F{sub 1}-{alpha}/{beta} subunits inhibits the ATP-driven H{sup +} translocation but enhances H{sup +} conduction in the reverse direction. These observation are discussed in terms of the rotary mechanism of the F{sub o}F{sub 1} complex.},
doi = {10.1016/J.BBRC.2009.04.046},
url = {https://www.osti.gov/biblio/22199720},
journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 1,
volume = 384,
place = {United States},
year = {Fri Jun 19 00:00:00 EDT 2009},
month = {Fri Jun 19 00:00:00 EDT 2009}
}