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

Mycobacterium tuberculosis MtrAY102C is a gain-of-function mutant that potentially acts as a constitutively active protein.

Tuberculosis (Edinburgh, Scotland) - 1 Dec 2013

Satsangi Akash T, Pandeeti Emmanuel P, Sarva Krishna, Rajagopalan Malini, Madiraju Murty V

Abstract excerpt

The MtrAB histidine-aspartate signal transduction of mycobacteria includes the response regulator MtrA and sensor kinase MtrB. We recently showed that Mycobacterium smegmatis ΔmtrB is filamentous, defective for cell division, cell shape maintenance and shows compromised MtrA target gene expression. Interestingly, overproduction of phosphorylation competent M. tuberculosis MtrAY102C reverses the ΔmtrB mutant...

Read the complete abstract on PubMed

Topics

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

Share to Asparagine
Share to Aspartic Acid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to ATP-Binding Cassette Transporters

Share to Cell Membrane

Share to Cell Wall

Share to Mycobacterium smegmatis

Share to Mycobacterium tuberculosis

Share to RNA-Binding Proteins

Source

Identifiers

PMID: 24388645
DOI: 10.1016/S1472-9792(13)70007-6

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

Mycobacterium tuberculosis MtrAY102C is a gain-of-function mutant that potentially acts as a constitutively active protein.PMID 24388645Read ↗

Septal localization of the Mycobacterium tuberculosis MtrB sensor kinase promotes MtrA regulon expression.Semantic proximity Read ↗

The sensor kinase MtrB of Mycobacterium tuberculosis regulates hypoxic survival and establishment of infectionSemantic proximity Read ↗

The MprB Extracytoplasmic Domain Negatively Regulates Activation of the Mycobacterium tuberculosis MprAB Two-Component SystemSemantic proximity Read ↗

Global mapping of MtrA-binding sites links MtrA to regulation of its targets in Mycobacterium tuberculosis.Semantic proximity Read ↗

M. tuberculosis PrrA binds the dosR promoter and regulates mycobacterial adaptation to hypoxia.Semantic proximity Read ↗

A high-frequency single nucleotide polymorphism in the MtrB sensor kinase in clinical strains of Mycobacterium tuberculosis alters its biochemical and physiological properties.Semantic proximity Read ↗

Mycobacterium tuberculosis supports protein tyrosine phosphorylation.Semantic proximity Read ↗

Phenotypic characterization of a novel double knockout PknI/DacB2 from Mycobacterium tuberculosis.Semantic proximity Read ↗

The Mycobacterium tuberculosis Ser/Thr kinase substrate Rv2175c is a DNA-binding protein regulated by phosphorylation.Semantic proximity Read ↗

Double deletion of PknI/DacB2 leads to attenuation of Mycobacterium tuberculosis for growth and virulence.Semantic proximity Read ↗

RD-1 encoded EspJ protein gets phosphorylated prior to affect the growth and intracellular survival of mycobacteria.Semantic proximity Read ↗

The prrAB two-component system is essential for Mycobacterium tuberculosis viability and is induced under nitrogen-limiting conditions.Semantic proximity Read ↗

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