Multiple layers of regulation determine the cellular levels of the Pup ligase PafA in Mycobacterium smegmatis.


Journal

Molecular microbiology
ISSN: 1365-2958
Titre abrégé: Mol Microbiol
Pays: England
ID NLM: 8712028

Informations de publication

Date de publication:
08 2019
Historique:
accepted: 15 05 2019
pubmed: 21 5 2019
medline: 12 5 2020
entrez: 21 5 2019
Statut: ppublish

Résumé

Despite being a destructive process, regulated protein degradation is fundamental for proper cell function. While regulated proteolysis in eukaryotes largely involves the ubiquitin-proteasome system (UPS), most bacterial species rely on multiple ATP-dependent proteases, such as the Clp proteases. Mycobacteria and related actinobacterial species also possess a degradation system analogous in its function to the UPS. In this system, a prokaryotic ubiquitin-like protein (Pup) is conjugated to proteins, thereby marking them for proteasomal degradation. A single ligase, PafA, is responsible for Pup conjugation to many protein targets, thus playing a central role in the Pup-proteasome system (PPS). In Mycobacterium smegmatis, a model mycobacterial organism where the PPS is essential under starvation conditions, cellular PafA levels change in response to nutrient availability. Indeed, increased PafA levels are observed upon nutrient limitation. We found that a multi-layered network involving transcriptional, translational and post-translational regulation determines cellular PafA levels. Induced expression is observed at stationary phase, whereas PafA degradation by the proteasome and ClpCP occurs in exponentially growing cells, as opposed to starved cells. In both growth stages, translation attenuation maintains low PafA expression levels. Altogether, these mechanisms establish the dynamics in PafA levels during bacterial growth.

Identifiants

pubmed: 31106455
doi: 10.1111/mmi.14278
doi:

Substances chimiques

Bacterial Proteins 0
Ubiquitin 0
Alkaline Phosphatase EC 3.1.3.1
periplasmic alkaline phosphatase, Chryseobacterium meningosepticum EC 3.1.3.1
Proteasome Endopeptidase Complex EC 3.4.25.1

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

620-631

Informations de copyright

© 2019 John Wiley & Sons Ltd.

Références

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Auteurs

Maayan Korman (M)

Department of Life Sciences, Ben-Gurion University of the Negev, Beer-Sheva, 84105, Israel.

Shai Schlussel (S)

Department of Life Sciences, Ben-Gurion University of the Negev, Beer-Sheva, 84105, Israel.

Marina Vishkautzan (M)

Department of Life Sciences, Ben-Gurion University of the Negev, Beer-Sheva, 84105, Israel.
The National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, Beer-Sheva, 84105, Israel.

Eyal Gur (E)

Department of Life Sciences, Ben-Gurion University of the Negev, Beer-Sheva, 84105, Israel.
The National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, Beer-Sheva, 84105, Israel.

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