Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Topology and proximity relationships of yeast mitochondrial ATP synthase subunit 8 determined by unique introduced cysteine residues.

European journal of biochemistry - 1 Nov 2000

Stephens A N, Roucou X, Artika I M, Devenish R J, Nagley P

Abstract excerpt

We have used site-directed chemical labelling to demonstrate the membrane topology and to identify neighbouring subunits of subunit 8 (Y8) in yeast mitochondrial ATP synthase (mtATPase). Unique cysteine residues were introduced at the N or C-terminus of Y8 by site-directed mutagenesis. Expression and targeting to mitochondria in vivo of each of these variants in a yeast Y8 null mutant was able to restore activity...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Respiration
Share to Cross-Linking Reagents

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Disulfides

Share to Protein Engineering

Share to Protein Structure, Quaternary

Share to Protein Subunits

Share to Proton-Translocating ATPases

Share to Yeasts

Source

Identifiers

PMID: 11029588
DOI: 10.1046/j.1432-1327.2000.01733.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Topology and proximity relationships of yeast mitochondrial ATP synthase subunit 8 determined by unique introduced cysteine residues.PMID 11029588Read ↗

The molecular neighborhood of subunit 8 of yeast mitochondrial F1F0-ATP synthase probed by cysteine scanning mutagenesis and chemical modification.Semantic proximity Read ↗

Molecular genetic analysis of the central hydrophobic domain of subunit 8 of yeast mitochondrial ATP synthase.Semantic proximity Read ↗

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

Bioenergetic and structural consequences of allotopic expression of subunit 8 of yeast mitochondrial ATP synthase. The hydrophobic character of residues 23 and 24 is essential for maximal activity and structural stability of the enzyme complex.Semantic proximity Read ↗

Organisation of the yeast ATP synthase F(0):a study based on cysteine mutants, thiol modification and cross-linking reagents.Semantic proximity Read ↗

Topography of the yeast ATP synthase F0 sector.Semantic proximity Read ↗

Insights into ATP synthase assembly and function through the molecular genetic manipulation of subunits of the yeast mitochondrial enzyme complex.Semantic proximity Read ↗

Assembly of imported subunit 8 into the ATP synthase complex of isolated yeast mitochondria.Semantic proximity Read ↗

Each yeast mitochondrial F1F0-ATP synthase complex contains a single copy of subunit 8.Semantic proximity Read ↗

Relationship of subunit 8 of yeast ATP synthase and the inner mitochondrial membrane. Subunit 8 variants containing multiple lysine residues in the central hydrophobic domain retain function.Semantic proximity Read ↗

The yeast F(1)F(0)-ATP synthase: analysis of the molecular organization of subunit g and the importance of a conserved GXXXG motif.Semantic proximity Read ↗

Characterization of loops of the yeast mitochondrial ADP/ATP carrier facing the cytosol by site-directed mutagenesis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.