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<i>Mycobacterium tuberculosis</i>GroEL1 Chaperone Is a Substrate of Ser/Thr Protein Kinases

7 Feb 2009

Abstract excerpt

We demonstrate that Mycobacterium tuberculosis GroEL1 is phosphorylated by PknF at two positions, Thr25 and Thr54. Unexpectedly, Mycobacterium smegmatis GroEL1 is not a substrate of its cognate PknF. This study shows that the phosphorylation profiles of conserved proteins are species dependent and provide insights that may explain the numerous biological functions of these important proteins.

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Genetics and Biotechnology
Share to Enzyme Structure and Function
Share to Tuberculosis Research and Epidemiology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 19201798
DOI: 10.1128/jb.01569-08

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The<i>Mycobacterium tuberculosis</i>GroEL1 Chaperone Is a Substrate of Ser/Thr Protein KinasesPMID 19201798Read ↗

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

Mycobacterium tuberculosis supports protein tyrosine phosphorylation.Semantic proximity Read ↗

Role of post‐translational modifications in the acquisition of drug resistance in <i>Mycobacterium tuberculosis</i>Semantic proximity Read ↗

Delineating the functional role of the <i>PPE50 (Rv3135) - PPE51 (Rv3136)</i> gene cluster in the pathophysiology of <i>Mycobacterium tuberculosis</i>Semantic proximity Read ↗

Relative and QuantitativePhosphoproteome Analysisof Macrophages in Response to Infection by Virulent and Avirulent <i>Mycobacteria</i> Reveals a Distinct Role of the Cytosolic RNASensor RIG‑I in <i>Mycobacterium tuberculosis</i> PathogenesisSemantic proximity Read ↗

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

Serine threonine protein kinases of mycobacterial genus: phylogeny to functionSemantic proximity Read ↗

The <i>PPE25 (Rv1787) - PE18 (Rv1788) - PPE26 (Rv1789)</i> gene cluster encodes an interacting protein pair and is involved in immune evasion by <i>Mycobacterium tuberculosis</i>Semantic proximity Read ↗

Staphylococcal PknB as the first prokaryotic representative of the proline-directed kinases.Semantic proximity Read ↗

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

Comparative proteome analysis of <i>Mycobacterium tuberculosis</i> and <i>Mycobacterium bovis</i> BCG strains: towards functional genomics of microbial pathogensSemantic proximity Read ↗

Identification of serine/threonine kinase substrates in the human pathogen group B streptococcus.Semantic proximity Read ↗

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