Evidence map›Paper›PMID 20507997›Full record

ArticleThe Journal of biological chemistry2010

cAMP-regulated protein lysine acetylases in mycobacteria.

Subhalaxmi Nambi, Nirmalya Basu, Sandhya S Visweswariah

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
3.5field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

67 citing papers in PubMed, 112 citations in OpenAlex.

  1. NProceedings of the National Academy of Sciences of the United States of America · 2025
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  2. Article
  3. Review
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  5. Cyclic AMP-Mediated Inhibition of Cholesterol Catabolism inAntimicrobial agents and chemotherapy · 2023
    Article
  6. The role ofFrontiers in cellular and infection microbiology · 2023
    Review
  7. Frontiers in immunology · 2023
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Post-translational Succinylation ofACS infectious diseases · 2020
    Article
  17. A universal stress protein inThe Journal of biological chemistry · 2020
    Article
  18. Acetylation of Response Regulator Protein MtrA inFrontiers in microbiology · 2020
    Article
  19. Article
  20. Protein Acetylation in Bacteria.Annual review of microbiology · 2019
    Review

7 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Subhalaxmi NambiDepartment of Molecular Reproduction, Development and Genetics, Indian Institute of Science, Bangalore 560012, India.
Nirmalya Basu
Sandhya S Visweswariah
Indian Institute of Science Bangalore · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclic AMP synthesized by Mycobacterium tuberculosis has been shown to play a role in pathogenesis. However, the high levels of intracellular cAMP found in both pathogenic and non-pathogenic mycobacteria suggest that additional and important biological processes are regulated by cAMP in these organisms. We describe here the biochemical characterization of novel cAMP-binding proteins in M. smegmatis and M. tuberculosis (MSMEG_5458 and Rv0998, respectively) that contain a cyclic nucleotide binding domain fused to a domain that shows similarity to the GNAT family of acetyltransferases. We detect protein lysine acetylation in mycobacteria and identify a universal stress protein (USP) as a substrate of MSMEG_5458. Acetylation of a lysine residue in USP is regulated by cAMP, and using a strain deleted for MSMEG_5458, we show that USP is indeed an in vivo substrate for MSMEG_5458. The Rv0998 protein shows a strict cAMP-dependent acetylation of USP, despite a lower affinity for cAMP than MSMEG_5458. Thus, this report not only represents the first demonstration of protein lysine acetylation in mycobacteria but also describes a unique functional interplay between a cyclic nucleotide binding domain and a protein acetyltransferase.

Indexed as

AcetylationAcetylesteraseAllosteric SiteAmino Acid SequenceCloning, MolecularCyclic AMPLysineModels, BiologicalMolecular Sequence DataMutagenesisMycobacterium tuberculosisPhylogenyProtein BindingSequence Homology, Amino AcidSignal TransductionAcetylesteraseCyclic AMPLysine

Identifiers

PMID20507997
PMCPMC2915667
OpenAlexW2059473902

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.