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

The α10 helix of DevR, the Mycobacterium tuberculosis dormancy response regulator, regulates its DNA binding and activity.

The FEBS journal - 1 Apr 2016

Vashist Atul, Prithvi Raj D, Gupta Umesh Datta, Bhat Rajiv, Tyagi Jaya Sivaswami

Abstract excerpt

The crystal structures of several bacterial response regulators provide insight into the various interdomain molecular interactions potentially involved in maintaining their 'active' or 'inactive' states. However, the requirement of high concentrations of protein, an optimal pH and ionic strength buffers during crystallization may result in a structure somewhat different from that observed in solution. Therefore,...

Read the complete abstract on PubMed

Topics

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

Share to Anaerobiosis
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Bacterial

Share to Mycobacterium tuberculosis

Share to Protein Folding

Share to Protein Kinases

Share to Protein Structure, Secondary

Share to Temperature

Source

Identifiers

PMID: 26799615
DOI: 10.1111/febs.13664

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

The α10 helix of DevR, the Mycobacterium tuberculosis dormancy response regulator, regulates its DNA binding and activity.PMID 26799615Read ↗

Essentiality of DevR/DosR Interaction with SigA for the Dormancy Survival Program in Mycobacterium tuberculosisSemantic proximity Read ↗

Cooperative binding of phosphorylated DevR to upstream sites is necessary and sufficient for activation of the Rv3134c-devRS operon in Mycobacterium tuberculosis: implication in the induction of DevR target genes.Semantic proximity Read ↗

Phosphatase-defective DevS sensor kinase mutants permit constitutive expression of DevR-regulated dormancy genes in Mycobacterium tuberculosis.Semantic proximity Read ↗

Appropriate DevR (DosR)-mediated signaling determines transcriptional response, hypoxic viability and virulence of Mycobacterium tuberculosis.Semantic proximity Read ↗

DevR–DevS is a bona fide two-component system of Mycobacterium tuberculosis that is hypoxia-responsive in the absence of the DNA-binding domain of DevRSemantic proximity Read ↗

Molecular analysis of the dormancy response inMycobacterium smegmatis: expression analysis of genes encoding the DevR–DevS two-component system, Rv3134c and chaperone α-crystallin homologuesSemantic proximity Read ↗

DevS/DosS sensor is bifunctional and its phosphatase activity precludes aerobic DevR/DosR regulon expression in Mycobacterium tuberculosis.Semantic proximity Read ↗

Mycobacterium tuberculosis DosR Regulon Gene Rv0079 Encodes a Putative, ‘Dormancy Associated Translation Inhibitor (DATIN)’Semantic proximity Read ↗

Co-expression of DevR and DevR(N)-Aph proteins is associated with hypoxic adaptation defect and virulence attenuation of Mycobacterium tuberculosis.Semantic proximity Read ↗

A two-component regulator of universal stress protein expression and adaptation to oxygen starvation in Mycobacterium smegmatis.Semantic proximity Read ↗

Structural basis of hypoxic gene regulation by the Rv0081 transcription factor of <i>Mycobacterium tuberculosis</i>Semantic proximity Read ↗

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

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