Fluctuation of the First Loop Facing the Matrix of the Mitochondrial ADP/ATP Carrier Deduced from Intermolecular Cross-Linking of Cys56 Residues by Bifunctional Dimaleimides
Abstract
The effects of six thiol-specific cross-linker dimaleimides, in which the distance of the two maleimide groups ranged from 7.7 to 16. 8 A, on bovine heart mitochondria were studied at pH 7.2 and 0 degrees C. None of the dimaleimides affected mitochondrial proteins, but they caused significantly specific intermolecular cross-linking of the 30 kDa ADP/ATP carrier in submitochondrial particles. All the cross-links were found to be formed specifically between two Cys56 residues in the first loop facing the matrix, as we observed previously in intermolecular disulfide bridge formation catalyzed by copper o-phenanthroline [Majima, E., Ikawa, K., Takeda, M., Hashimoto, M., Shinohara, Y., and Terada, H. (1995) J.Biol. Chem. 270, 29548-29554]. The dimerization was dependent on the cross-linking span of the dimaleimides, being maximum with the dimaleimide having a span of about 12 A. Cross-linking took place in the m-state carrier, but not in the c-state carrier, and inhibited ADP transport via the ADP/ATP carrier. We suggest that a pair of first loops with Cys56 residues in the dimer form of the m-state carrier fluctuates widely with a most probable distance between them of about 12 A, and that this fluctuation modulates the transport activity of the ADP/ATP carrier.
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Cys57 can be induced to form an intermolecular disulfide between ANT subunits only when ANT is in the m state but not the c state.
“The third thiol, Cys57, can be induced to form an intermolecular disulfide between ANT subunits only when it is in the “m” state but not the “c” state, confirming the proximity of these residues in the functional homodimer;”
From Redox regulation of mitochondrial function (2012) · cites this paper as [171]
These ANT dimers block transport function.
“however, these dimers also block transport function (171).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [171]
ANT has three thiols implicated in its function that are located in three distinct hydrophilic loops.
“ANT has three thiols that are implicated in its function that are located in three distinct hydrophilic loops (102, 167, 171, 286).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [171]
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- Authors
- Hashimoto, M., Majima, E., Goto, S., Shinohara, Y., & Terada, H.
- Affiliations
- Tokushima University (JP)
- Corresponding author
- Terada, Hiroshi
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1998-12-30
- Volume
- 38
- Issue
- 3
- Pages
- 1050-1056
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2028814041
- Cited by
- 53
- References
- 8
- Citations by year
- 2025: 1 · 2023: 1 · 2022: 2 · 2020: 2 · 2017: 2 · 2016: 2 · 2013: 1 · 2012: 3
- FWCI
- 0.81
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- mitochondrial ADP/ATP carrier, protein dimerization, submitochondrial particles, disulfide bond formation, protein conformational change
- MeSH terms
- Mitochondrial ADP, ATP Translocases, Adenosine Diphosphate, Animals, Biological Transport, Cattle, Cross-Linking Reagents, Cysteine, Ethylmaleimide, Glutathione, Maleimides, Mitochondria, Heart, Protein Conformation, Solutions, Submitochondrial Particles
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