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

A triple mutation in the a subunit of the Escherichia coli/Propionigenium modestum F1Fo ATPase hybrid causes a switch from Na+ stimulation to Na+ inhibition.

Biochemistry - 31 Mar 1998

Kaim G, Dimroth P

Abstract excerpt

Previously we have shown that the Na+-translocating Escherichia coli (F1-delta)/Propionigenium modestum (Fo+delta) hybrid ATPase acquires a Na+-independent phenotype by the c subunit double mutation F84L, L87V that is reflected by Na+-independent growth of the mutant strain MPC8487 on succinate [Kaim, G., and Dimroth, P. (1995) J. Mol. Biol. 253, 726-738]. Here we describe a new class of mutants that were...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Bacterial Proteins
Share to Escherichia coli

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Plasmids

Share to Recombinant Proteins

Share to Sequence Analysis, DNA

Source

Identifiers

PMID: 9521783
DOI: 10.1021/bi973022f

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A triple mutation in the a subunit of the Escherichia coli/Propionigenium modestum F1Fo ATPase hybrid causes a switch from Na+ stimulation to Na+ inhibition.PMID 9521783Read ↗

Mode of interaction of the single a subunit with the multimeric c subunits during the translocation of the coupling ions by F1F0 ATPases.Semantic proximity Read ↗

Formation of a functionally active sodium-translocating hybrid F1F0 ATPase in Escherichia coli by homologous recombination.Semantic proximity Read ↗

Molecular mechanism of the ATP synthase's F(o) motor probed by mutational analyses of subunit a.Semantic proximity Read ↗

Coupling ion specificity of chimeras between H(+)- and Na(+)-driven motor proteins, MotB and PomB, in Vibrio polar flagella.Semantic proximity Read ↗

A Bacillus flagellar motor that can use both Na+ and K+ as a coupling ion is converted by a single mutation to use only Na+.Semantic proximity Read ↗

On the way towards the Na(+)-binding site within the F1F0 ATPase of Propionigenium modestum.Semantic proximity Read ↗

Three putative cation/proton antiporters from the soda lake alkaliphile Alkalimonas amylolytica N10 complement an alkali-sensitive Escherichia coli mutant.Semantic proximity Read ↗

MH1, a second-site revertant of an Escherichia coli mutant lacking Na+/H+ antiporters (delta nhaA delta nhaB), regains Na+ resistance and a capacity to excrete Na+ in a delta microH(+)-independent fashion.Semantic proximity Read ↗

Suppressor mutations in F1 subunit epsilon recouple ATP-driven H+ translocation in uncoupled Q42E subunit c mutant of Escherichia coli F1F0 ATP synthase.Semantic proximity Read ↗

NhaA Na+/H+ antiporter mutants that hardly react to the membrane potential.Semantic proximity Read ↗

Molecular cloning and sequencing of a gene from alkaliphilic Bacillus firmus OF4 that functionally complements an Escherichia coli strain carrying a deletion in the nhaA Na+/H+ antiporter gene.Semantic proximity Read ↗

Mutants of Streptococcus faecalis sensitive to alkaline pH lack Na(+)-ATPase.Semantic proximity Read ↗

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