ArticleArchives of biochemistry and biophysics2008
The proximal N-terminal amino acid residues are required for the coupling activity of the bovine heart mitochondrial factor B.
Article in Archives of biochemistry and biophysics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 10 citations in OpenAlex.
- Genome evolution in the cold: Antarctic icefish muscle transcriptome reveals selective duplications increasing mitochondrial function.Genome biology and evolution · 2013Article
- Coupling factor B affects the morphology of mitochondria.Journal of bioenergetics and biomembranes · 2010Article
- Cyclophilin D modulates mitochondrial F0F1-ATP synthase by interacting with the lateral stalk of the complex.The Journal of biological chemistry · 2009Article
- Recent advances in structure-functional studies of mitochondrial factor B.Journal of bioenergetics and biomembranes · 2009Review
- Mitochondrial and cell-surface F0F1ATPsynthase in innate and acquired cardioprotection.Journal of bioenergetics and biomembranes · 2009Review
- Crystal structure of bovine mitochondrial factor B at 0.96-A resolution.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Functional and stoichiometric analysis of subunit e in bovine heart mitochondrial F(0)F(1)ATP synthase.Journal of bioenergetics and biomembranes · 2008Article
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1 author at 1 institution in 1 country.
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Abstract
Treatment of the recombinant bovine factor B with trypsin yielded a fragment (amino acid residues 62-175) devoid of coupling activity. Removal of the N-terminal Trp2-Gly3-Trp4 peptide resulted in a significant loss of coupling activity in the FB(DeltaW)(2)(-W)(4) deletion mutant. Sucrose density gradient centrifugation demonstrated co-sedimentation of recombinant factor B with the ADP/ATP carrier, which is present in preparations of H(+)-translocating F(0)F(1)-ATPase, but not in preparations of complex V. The N-terminally truncated factor B mutant FB(DeltaW)(2)(-W)(4) did not co-sediment with the ADP/ATP carrier. Recombinant factor B co-sedimented with partially purified membrane sector F(0), extracted from F(1)-stripped bovine submitochondrial particles with n-dodecyl-beta-d-maltoside. Factor B inhibited the passive proton conductance catalyzed by F(0) reconstituted into asolectin liposomes. A factor B mutant, bearing a photoreactive unnatural amino acid pbenzoyl-l-phenylalanine (pBpa) substituted for Trp2, cross-linked with F(0) subunits e and g as well as the ADP/ATP carrier. These results suggest that the N-terminal domain and, in particular, the proximal N-terminal amino acids are important for the coupling activity and protein-protein interactions of bovine factor B.
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