Evidence map›Paper›PMID 22773105›Full record

ArticleNature structural & molecular biology2012

Cyclic AMP regulation of protein lysine acetylation in Mycobacterium tuberculosis.

Ho Jun Lee, P Therese Lang, Sarah M Fortune, Christopher M Sassetti, Tom Alber

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

39 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. NProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Structural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Review
  6. Cyclic AMP-Mediated Inhibition of Cholesterol Catabolism inAntimicrobial agents and chemotherapy · 2023
    Article
  7. Frontiers in immunology · 2023
    Review
  8. Article
  9. Review
  10. Review
  11. Review
  12. A universal stress protein inThe Journal of biological chemistry · 2020
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. NJournal of proteome research · 2017
    Article
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

5 authors at 3 institutions in 1 country.

Ho Jun LeeDepartment of Molecular and Cell Biology, University of California, Berkeley, California, USA.
P Therese Lang
Sarah M Fortune
Christopher M Sassetti
Tom Alber
University of California, Berkeley · USHarvard University · USUniversity of Massachusetts Chan Medical School · US

Funding

The Cloning Protein Production, Crystallization, and X-ray Data Collection CoreP01AI068135 · NIAID · TEXAS A&M AGRILIFE RESEARCH · PI ALBER, THOMAS C · 2006 to 2010
$13.2M
Functions and Mechanisms of M. Tuberculosis S/T KinasesR01GM070962 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI ALBER, THOMAS C · 2005 to 2012
$2.2M
CIHRNIAID NIH HHS P01 AI068135NIAID NIH HHS P01AI068135NIGMS NIH HHS R01 GM070962NIGMS NIH HHS R01GM70962
6 · The paper itself

Abstract

Protein lysine acetylation networks can regulate central processes such as carbon metabolism and gene expression in bacteria. In Escherichia coli, cyclic AMP (cAMP) regulates protein lysine acetyltransferase (PAT) activity at the transcriptional level, but in Mycobacterium tuberculosis, fusion of a cyclic nucleotide-binding domain to a Gcn5-like PAT domain enables direct cAMP control of protein acetylation. Here we describe the allosteric activation mechanism of M. tuberculosis PAT. The crystal structures of the autoinhibited and cAMP-activated PAT reveal that cAMP binds to a cryptic site in the regulatory domain that is over 32 Å from the catalytic site. An extensive conformational rearrangement relieves this autoinhibition by means of a substrate-mimicking lid that covers the protein-substrate binding surface. A steric double latch couples the domains by harnessing a classic, cAMP-mediated conformational switch. The structures suggest general features that enable the evolution of long-range communication between linked domains.

Indexed as

AcetylationAcetyltransferasesBacterial ProteinsBinding SitesCatalytic DomainCrystallography, X-RayCyclic AMPLigandsLysineModels, MolecularMutagenesisMycobacterium tuberculosisProtein ConformationProtein Structure, TertiaryAcetyltransferasesBacterial ProteinsCyclic AMPLigandsLysine

Identifiers

PMID22773105
PMCPMC3414669
OpenAlexW2102510233

What OpenQuestion holds

Textmetadata
LicenceTDM
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.