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Cited by 44Lipid metabolism and biosynthesisTuberculosis Research and EpidemiologyCancer, Lipids, and Metabolism

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Negative regulation by Ser/Thr phosphorylation of HadAB and HadBC dehydratases from Mycobacterium tuberculosis type II fatty acid synthase system

Slama, Nawel, Leiba, Jade, Eynard, Nathalie, Daffé, Mamadou, Kremer, Laurent, Quémard, Annaïk, Molle, Virginie·2011·Biochemical and Biophysical Research Communications
DOI 10.1016/j.bbrc.2011.07.051
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Abstract

The type II fatty acid synthase system of mycobacteria is involved in the biosynthesis of major and essential lipids, mycolic acids, key-factors of Mycobacterium tuberculosis pathogenicity. One reason of the remarkable survival ability of M. tuberculosis in infected hosts is partly related to the presence of cell wall-associated mycolic acids. Despite their importance, the mechanisms that modulate synthesis of these lipids in response to environmental changes are unknown. We demonstrate here that HadAB and HadBC dehydratases of this system are phosphorylated by Ser/Thr protein kinases, which negatively affects their enzymatic activity. The phosphorylation of HadAB/BC is growth phase-dependent, suggesting that it represents a mechanism by which mycobacteria might tightly control mycolic acid biosynthesis under non-replicating condition.

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  • The FAS-II enzymes are all inhibited through phosphorylation by PknA, PknB and other STPKs.

    “The FAS-​II enzymes are all inhibited through phosphorylation by PknA, PknB and other STPKs89–93.”

    From The mycobacterial cell envelope — a moving target (2020) · cites this paper as [91]

  • PknH, PknD, PknL and PknF can also phosphorylate various FAS-II enzymes.

    “PknH, PknD, PknL and PknF can also phosphorylate various FAS-​II enzymes.”

    From The mycobacterial cell envelope — a moving target (2020) · cites this paper as [91]

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Cited by

Sorted by citations

Metadata

Authors
Slama, N., Leiba, J., Eynard, N., Daffé, M., Kremer, L., Quémard, A., & Molle, V.
Affiliations
Centre National de la Recherche Scientifique (FR)
Corresponding author
Molle, Virginie
ORCID
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
2011-09
Volume
412
Issue
3
Pages
401-406
ISSN
0006-291X (ISSN-L)
DOI
10.1016/j.bbrc.2011.07.051
OpenAlex
W1993827593
Cited by
44
References
1
Citations by year
2026: 1 · 2025: 2 · 2022: 1 · 2020: 3 · 2019: 4 · 2018: 2 · 2017: 8 · 2016: 5 · 2015: 5 · 2014: 5 · 2013: 4 · 2012: 4
FWCI
1.76
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Biochemical and Biophysical Research Communications (publishedVersion)
  • PubMed (publishedVersion)
  • HAL (submittedVersion)
Funders
  • European Community
  • National Research Agency
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
  • Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
Keywords
Mycobacterium tuberculosis, type II fatty acid synthase, dehydratase, kinase regulation, mycolic acid biosynthesis, non-replicating mycobacteria, growth phase regulation, lipid biosynthesis regulation
MeSH terms
Amino Acid Sequence, Hydro-Lyases, Molecular Sequence Data, Mycobacterium tuberculosis, Phosphorylation, Serine, Threonine, Down-Regulation, Fatty Acid Synthase, Type II

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