2003
DOI: 10.1074/jbc.m300967200
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The Molecular Neighborhood of Subunit 8 of Yeast Mitochondrial F1F0-ATP Synthase Probed by Cysteine Scanning Mutagenesis and Chemical Modification

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Cited by 38 publications
(38 citation statements)
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“…This residue, which is non-conserved, was susceptible to cross-linking from the intermembrane space with three components of the peripheral stalk (subunits 4, 8, and i) that are located in its neighborhood (29,43,44). In this work, we found that a cross-linking product involving subunit 6 and showing a relative mass of 47,000 was obtained upon incubation of wild-type mitochondria with CuCl 2 (Fig.…”
Section: Resultsmentioning
confidence: 52%
See 1 more Smart Citation
“…This residue, which is non-conserved, was susceptible to cross-linking from the intermembrane space with three components of the peripheral stalk (subunits 4, 8, and i) that are located in its neighborhood (29,43,44). In this work, we found that a cross-linking product involving subunit 6 and showing a relative mass of 47,000 was obtained upon incubation of wild-type mitochondria with CuCl 2 (Fig.…”
Section: Resultsmentioning
confidence: 52%
“…Subunit 6 is located in the periphery of the ATP synthase in contact with the membranous rotor with which it forms the proton channel. It belongs to the peripheral stalk of the ATP synthase and likely interacts with other components of the stalk such as subunits 4 (b), i, and 8, as shown by cross-linking experiments (29,43,44). In this work, we produced a disulfide bridge between two subunits 6 via their Cys 23 upon oxidation of either mitochondria or the solubilized supramolecular forms of ATP synthase.…”
mentioning
confidence: 99%
“…ATP6 and ATP8 are the two mtDNA-encoded subunits that are incorporate into Complex V where they play essential roles in the final assembly of ATPase [52,62]. Studies in yeast demonstrated that the N-terminal signal-peptide domain of ATP8 is responsible for its function [63], whereas the C-terminal domain is required for the assembly of F 0 [64] and the transmembrane stem accommodates charged AA residues [65]. The Artemia ATP8 proteins shares a common four-residue sequence motif (IPQM) at their N-termini, which is similar to the ATP8-specific motif (MPQM) identified previously in other animals [66].…”
Section: Protein-coding Genesmentioning
confidence: 99%
“…The addition of Atp6p at a late stage of assembly may prevent the exchange of protons across the membrane through the partially assembled F 0 sector. This scheme is still very fragmentary and is lacking a host of intermolecular interactions of other F 0 subunits needed to stabilize the final complex (1,2,13).…”
mentioning
confidence: 99%