Topography of the yeast ATP synthase F0 sector by using cysteine substitution mutants. Cross-linkings between subunits 4, 6, and f

Biochemistry. 1998 Jan 13;37(2):615-21. doi: 10.1021/bi9714971.

Abstract

The arrangement of the N-terminal part of subunit 4 (subunit b) has been studied by the use of mutants containing cysteine residues in a loop connecting the two N-terminal postulated membrane-spanning segments. Labelling of the mutated subunit 4 by the fluorescent probe N-(7-(dimethylamino)-4-methyl-3-coumarinyl)maleimide revealed that the sulfhydryl groups were modified upon incubation of intact mitochondria. In addition, the nonpermeant sulfhydryl reagent 4-acetamido-4'-maleimidylstilbene-2,2'-disulfonic acid prevented the 3-(N-maleimidylpropionyl)biocytin labeling of subunit 4D54C, thus showing a location of this residue in the intermembrane space. Cross-linking experiments revealed the proximity of subunits 4 and f. In addition a disulfide bridge between subunit 4D54C and subunit 6 was evidenced, thus demonstrating near-neighbor relationships of the two subunits and a location of the N-terminal part of the mitochondrially-encoded subunit 6 in the intermembrane space.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cross-Linking Reagents
  • Cysteine / genetics
  • Fluorescent Dyes
  • Maleimides
  • Molecular Sequence Data
  • Mutation
  • Peptide Fragments / chemistry
  • Peptide Fragments / genetics
  • Protein Conformation
  • Proton-Translocating ATPases / chemistry*
  • Proton-Translocating ATPases / genetics
  • Saccharomyces cerevisiae / enzymology*
  • Sulfhydryl Reagents

Substances

  • Cross-Linking Reagents
  • Fluorescent Dyes
  • Maleimides
  • Peptide Fragments
  • Sulfhydryl Reagents
  • Proton-Translocating ATPases
  • Cysteine