Evidence map›Paper›PMID 20472794›Full record

ArticleJournal of bacteriology2010

Redundant function of cmaA2 and mmaA2 in Mycobacterium tuberculosis cis cyclopropanation of oxygenated mycolates.

Daniel Barkan, Vivek Rao, George D Sukenick, Michael S Glickman

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.1field-weighted citation impact, top 21% 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

29 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
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  9. Glby, Encoded byJournal of bacteriology · 2022
    Article
  10. Cyclopropane Fatty Acids Are Important forInfection and immunity · 2022
    Article
  11. Review
  12. Review
  13. Review
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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

4 authors at 2 institutions in 1 country.

Daniel BarkanDivision of Infectious Diseases, Memorial Sloan Kettering Cancer Center, New York, New York 10065, USA.
Vivek Rao
George D Sukenick
Michael S Glickman
Office of Infectious Diseases · USMemorial Sloan Kettering Cancer Center · US

Funding

Cyclopropane Synthetases and M.tuerculosis VirulenceR01AI053417 · NIAID · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI GLICKMAN, MICHAEL S · 2003 to 2012
$3.9M
NIAID NIH HHS AI53417NIAID NIH HHS R01 AI053417
6 · The paper itself

Abstract

The Mycobacterium tuberculosis cell envelope contains a wide variety of lipids and glycolipids, including mycolic acids, long-chain branched fatty acids that are decorated by cyclopropane rings. Genetic analysis of the mycolate methyltransferase family has been a powerful approach to assign functions to each of these enzymes but has failed to reveal the origin of cis cyclopropanation of the oxygenated mycolates. Here we examine potential redundancy between mycolic acid methyltransferases by generating and analyzing M. tuberculosis strains lacking mmaA2 and cmaA2, mmaA2 and cmaA1, or mmaA1 alone. M. tuberculosis lacking both cmaA2 and mmaA2 cannot cis cyclopropanate methoxymycolates or ketomycolates, phenotypes not shared by the mmaA2 and cmaA2 single mutants. In contrast, a combined loss of cmaA1 and mmaA2 had no effect on mycolic acid modification compared to results with a loss of mmaA2 alone. Deletion of mmaA1 from M. tuberculosis abolishes trans cyclopropanation without accumulation of trans-unsaturated oxygenated mycolates, placing MmaA1 in the biosynthetic pathway for trans-cyclopropanated oxygenated mycolates before CmaA2. These results define new functions for the mycolic acid methyltransferases of M. tuberculosis and indicate a substantial redundancy of function for MmaA2 and CmaA2, the latter of which can function as both a cis and trans cyclopropane synthase for the oxygenated mycolates.

Indexed as

Bacterial ProteinsGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicMethyltransferasesMycobacterium tuberculosisMycolic AcidsOxygenBacterial ProteinsCmaA2 protein, Mycobacterium tuberculosisMethyltransferasesMycolic AcidsOxygen

Identifiers

PMID20472794
PMCPMC2897352
OpenAlexW2087000626

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.