Browse
Submit Data
Databases
API
Help

Dataset Information

7 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Residue aspartate-147 from the third transmembrane region of Na(+)/H(+) antiporter NhaB of Vibrio alginolyticus plays a role in its activity.

ABSTRACT: NhaB is a bacterial Na(+)/H(+) antiporter with unique topology. The pH dependence of NhaB from Vibrio alginolyticus differs from that of the Escherichia coli NhaB homolog. Replacement of Asp-147 with Glu made high H(+) concentrations a requirement for the NhaB activity. Replacement of Asp-147 with neutral amino acids inactivated NhaB.

SUBMITTER: Nakamura T

PROVIDER: S-EPMC95471 | biostudies-literature | 2001 Oct

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Residue aspartate-147 from the third transmembrane region of Na(+)/H(+) antiporter NhaB of Vibrio alginolyticus plays a role in its activity.

Nakamura T T Fujisaki Y Y Enomoto H H Nakayama Y Y Takabe T T Yamaguchi N N Uozumi N N

Journal of bacteriology 20011001 19

NhaB is a bacterial Na(+)/H(+) antiporter with unique topology. The pH dependence of NhaB from Vibrio alginolyticus differs from that of the Escherichia coli NhaB homolog. Replacement of Asp-147 with Glu made high H(+) concentrations a requirement for the NhaB activity. Replacement of Asp-147 with neutral amino acids inactivated NhaB. ...[more]

PMID: 11544242

Similar Datasets

RNA-Seq of Vibrio alginolyticus: Vibrio alginolyticus 18672

Project description:RNA-seq analysis demonstrated that VqsA (18672) controls ~275 genes' expression in V. alginolyticus. Collectively, our data established that VqsA plays essential roles in QS regulation and may facilitate the illumination of the mechanisms bacterial cells sense environmental signals and integrate them into coordinated QS responses.

2021-12-06 | GSE125760 | GEO

NhaA, an Na(+)/H(+) antiporter involved in environmental survival of Vibrio cholerae.

Project description:Vibrio cholerae, the agent of cholera, is a normal inhabitant of aquatic environments, in which it survives under a wide range of conditions of pH and salinity. In this work, we identified the nhaA gene in a wild-type epidemic strain of V. cholerae O1. nhaA encodes a protein of 382 amino acids that is very similar to the proteins NhaA of Vibrio parahaemolyticus, Vibrio alginolyticus ( approximately 87% identity), and Escherichia coli (56% identity). V. cholerae NhaA complements an E. coli nhaA mutant, enabling it to grow in 700 mM NaCl, pH 7.5, indicating functional homology to E. coli NhaA. However, unlike E. coli, the growth of a nhaA-inactivated mutant of V. cholerae was not restricted at various pH and NaCl concentrations, although it was inhibited in the presence of 120 mM LiCl at pH 8.5. Nevertheless, using a nhaA'-lacZ transcriptional fusion, we observed induction of nhaA transcription by Na(+), Li(+), and K(+). These results strongly suggest that NhaA is an Na(+)/H(+) antiporter contributing to the Na(+)/H(+) homeostasis of V. cholerae. nhaA-related sequences were detected in all strains of V. cholerae from the various serogroups. This gene is presumably involved in the survival and persistence of free-living bacteria in their natural habitat.

| S-EPMC102005 | biostudies-literature

EHUA Vibrio alginolyticus EPGS Nimblegen

Project description:Vibrio alginolyticus is a Gram-negative marine bacterium. A limited population of the organisms causes acute gastroenteritis in humans. In this study, Vibrio alginolyticus wild type strain EPGS is compared with the mutants of Ser-Thr kinase PpkA and phosphatase PppA, after cultured for 7h, in Luria-Bertani containing medium 3 % NaCl at 30 C. Our goal is to determine the ppkA and pppA regulon.

2011-12-31 | GSE24319 | GEO

Structure of the archaeal Na+/H+ antiporter NhaP1 and functional role of transmembrane helix 1.

Project description:We have determined the structure of the archaeal sodium/proton antiporter NhaP1 at 7 Å resolution by electron crystallography of 2D crystals. NhaP1 is a dimer in the membrane, with 13 membrane-spanning ?-helices per protomer, whereas the distantly related bacterial NhaA has 12. Dimer contacts in the two antiporters are very different, but the structure of a six-helix bundle at the tip of the protomer is conserved. The six-helix bundle of NhaA contains two partially unwound ?-helices thought to harbour the ion-translocation site, which is thus similar in NhaP1. A model of NhaP1 based on detailed sequence comparison and the NhaA structure was fitted to the 7 Å map. The additional N-terminal helix 1 of NhaP1, which appears to be an uncleaved signal sequence, is located near the dimer interface. Similar sequences are present in many eukaryotic homologues of NhaP1, including NHE1. Although fully folded and able to dimerize, NhaP1 constructs without helix 1 are inactive. Possible reasons are investigated and discussed.

| S-EPMC3025466 | biostudies-literature

Transmembrane segment II of NhaA Na+/H+ antiporter lines the cation passage, and Asp65 is critical for pH activation of the antiporter.

Project description:The crystal structure of Escherichia coli NhaA determined at pH 4 has provided insights into the mechanism of activity of a pH-regulated Na+/H+ antiporter. However, because NhaA is activated at physiological pH (pH 5.5-8.5), many questions related to the active state of NhaA have remained elusive. Our experimental results at physiological pH and computational analyses reveal that amino acid residues in transmembrane segment II contribute to the cation pathway of NhaA and its pH regulation: 1) transmembrane segment II is a highly conserved helix and the conserved amino acid residues are located on one side of the helix facing either the cytoplasmic or periplasmic funnels of NhaA structure. 2) Cys replacements of the conserved residues and measuring their antiporter activity in everted membrane vesicles showed that D65C, L67C, E78C, and E82C increased the apparent K(m) to Na+ and Li+ and changed the pH response of the antiporter. 3) Introduced Cys replacements, L60C, N64C, F71C, F72C, and E78C, were significantly alkylated by [14C]N-ethylmaleimide implying the presence of water-filled cavities in NhaA. 4) Several Cys replacements were modified by MTSES and/or MTSET, membrane impermeant, negatively and positively charged reagents, respectively, that could reach Cys replacements from the periplasm only via water-filled funnel(s). Remarkably, the reactivity of D65C to MTSES increased with increasing pH and chemical modification by MTSES but not by MTSET, decreased the apparent K(m) of the antiporter at pH 7.5 (10-fold) but not at pH 8.5, implying the importance of Asp(65) negative charge for pH activation of the antiporter.

| S-EPMC2804377 | biostudies-literature

Ethanolamine utilization in Vibrio alginolyticus.

Project description:UnlabelledEthanolamine is used as an energy source by phylogenetically diverse bacteria including pathogens, by the concerted action of proteins from the eut-operon. Previous studies have revealed the presence of eutBC genes encoding ethanolamine-ammonia lyase, a key enzyme that breaks ethanolamine into acetaldehyde and ammonia, in about 100 bacterial genomes including members of gamma-proteobacteria. However, ethanolamine utilization has not been reported for any member of the Vibrio genus. Our comparative genomics study reveals the presence of genes that are involved in ethanolamine utilization in several Vibrio species. Using Vibrio alginolyticus as a model system we demonstrate that ethanolamine is better utilized as a nitrogen source than as a carbon source.ReviewersThis article was reviewed by Dr. Lakshminarayan Iyer and Dr. Vivek Anantharaman (nominated by Dr. L Aravind).

| S-EPMC3542024 | biostudies-literature

EHUA Vibrio alginolyticus EPGS Nimblegen

2011-12-31 | E-GEOD-24319 | biostudies-arrayexpress

Vibrio alginolyticus iTRAQ

Project description:In recent years, due to the influence of climate change and rising sea temperature, the incidence of Vibrio alginolyticus infections is increasing, and becoming the second most common Vibrio species reported in human illness. Therefore, better understanding of the pathogenic mechanism of V. alginolyticus infection is urgently needed. Vvrr1 (Vibrio virulence regulatory RNA 1) is a new found ncRNA predicted to be closely related to the adhesion ability of V. alginolyticus through the previous RNA-seq. In this study, the target genes of Vvrr1 were fully screened and verified by constructing Vvrr1 over-expressed strains and proteome sequencing technology.

2020-05-26 | PXD014375 | Pride

Vibrio alginolyticus 12G01 (wide type; NCBI:txid314288)

Project description: Not available

| S-MBRS2 | biostudies-other

Interaction of the C-terminal tail of FliF with FliG from the Na+-driven flagellar motor of Vibrio alginolyticus.

Project description:Rotation of the polar flagellum of Vibrio alginolyticus is driven by a Na(+)-type flagellar motor. FliG, one of the essential rotor proteins located at the upper rim of the C ring, binds to the membrane-embedded MS ring. The MS ring is composed of a single membrane protein, FliF, and serves as a foundation for flagellar assembly. Unexpectedly, about half of the Vibrio FliF protein produced at high levels in Escherichia coli was found in the soluble fraction. Soluble FliF purifies as an oligomer of ?700 kDa, as judged by analytical size exclusion chromatography. By using fluorescence correlation spectroscopy, an interaction between a soluble FliF multimer and FliG was detected. This binding was weakened by a series of deletions at the C-terminal end of FliF and was nearly eliminated by a 24-residue deletion or a point mutation at a highly conserved tryptophan residue (W575). Mutations in FliF that caused a defect in FliF-FliG binding abolish flagellation and therefore confer a nonmotile phenotype. As data from in vitro binding assays using the soluble FliF multimer correlate with data from in vivo functional analyses, we conclude that the C-terminal region of the soluble form of FliF retains the ability to bind FliG. Our study confirms that the C-terminal tail of FliF provides the binding site for FliG and is thus required for flagellation in Vibrio, as reported for other species. This is the first report of detection of the FliF-FliG interaction in the Na(+)-driven flagellar motor, both in vivo and in vitro.

| S-EPMC4288689 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data