Evidence map›Paper›PMID 27566542›Full record

ArticleThe Journal of biological chemistry2016

Post-translational Acetylation of MbtA Modulates Mycobacterial Siderophore Biosynthesis.

Olivia Vergnolle, Hua Xu, JoAnn M Tufariello, Lorenza Favrot, Adel A Malek, William R Jacobs, John S Blanchard

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.4field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

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  12. Rational inhibitor design for Pseudomonas aeruginosa salicylate adenylation enzyme PchD.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
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  16. A universal stress protein inThe Journal of biological chemistry · 2020
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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

7 authors at 2 institutions in 1 country.

Olivia VergnolleFrom the Department of Biochemistry and.
Hua XuFrom the Department of Biochemistry and.
JoAnn M Tufariellothe Department of Microbiology and Immunology, Howard Hughes Medical Institute, Albert Einstein College of Medicine, Bronx, New York 10461.
Lorenza FavrotFrom the Department of Biochemistry and.
Adel A Malekthe Department of Microbiology and Immunology, Howard Hughes Medical Institute, Albert Einstein College of Medicine, Bronx, New York 10461.
William R Jacobsthe Department of Microbiology and Immunology, Howard Hughes Medical Institute, Albert Einstein College of Medicine, Bronx, New York 10461.
John S BlanchardFrom the Department of Biochemistry and john.blanchard@einstein.yu.edu.
Howard Hughes Medical Institute · USAlbert Einstein College of Medicine · US

Funding

"The Tuberculous Granuloma"P01AI063537 · NIAID · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI CHAN, JOHN R. · 2005 to 2015
$15.7M
Molecular Genetic Analysis of Mycobacterium TuberculosisR37AI026170 · NIAID · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI WILLIAM Robert JACOBS · 2004 to 2026
$7.7M
Bacterial N-Acetyltransferases: Resistance to RegulationR01AI060899 · NIAID · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI BLANCHARD, JOHN S · 2004 to 2018
$7.7M
MOLECULAR GENETIC ANALYSIS OF MYCOBACTERIUM TUBERCULOSISR01AI026170 · NIAID · YESHIVA UNIVERSITY · PI JACOBS, WILLIAM ROBERT · 1989 to 2022
$7.1M
Vaccines for Extensively Drug Resistant TuberculosisR01AI098925 · NIAID · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI JACOBS, WILLIAM ROBERT · 2012 to 2016
$5.8M
NIAID NIH HHS P01 AI063537NIAID NIH HHS R01 AI026170NIAID NIH HHS R01 AI060899NIAID NIH HHS R01 AI098925NIAID NIH HHS R37 AI026170
6 · The paper itself

Abstract

Iron is an essential element for life, but its soluble form is scarce in the environment and is rarer in the human body. Mtb (Mycobacterium tuberculosis) produces two aryl-capped siderophores, mycobactin (MBT) and carboxymycobactin (cMBT), to chelate intracellular iron. The adenylating enzyme MbtA catalyzes the first step of mycobactin biosynthesis in two half-reactions: activation of the salicylic acid as an acyl-adenylate and ligation onto the acyl carrier protein (ACP) domain of MbtB to form covalently salicylated MbtB-ACP. We report the first apo-MbtA structure from Mycobacterium smegmatis at 2.3 Å. We demonstrate here that MbtA activity can be reversibly, post-translationally regulated by acetylation. Indeed the mycobacterial Pat (protein lysine acetyltransferase), Rv0998, specifically acetylates MbtA on lysine 546, in a cAMP-dependent manner, leading to enzyme inhibition. MbtA acetylation can be reversed by the NAD

Indexed as

AcetylationCatalysisHumansLigasesLysine AcetyltransferasesMycobacterium tuberculosisOxazolesProtein DomainsProtein Processing, Post-TranslationalSiderophoresLigasesLysine AcetyltransferasesmycobactinsOxazolessalicyl-AMP ligase, Mycobacterium tuberculosisSiderophoresacetylationenzyme structureironMbtAMycobacterium tuberculosismycobactinpost-translational modification (PTM)

Identifiers

PMID27566542
PMCPMC5064009
OpenAlexW2513660604

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.