Cited by 288Heat shock proteins researchBacterial Genetics and BiotechnologyBiochemical and Structural Characterization

Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram‐positive bacteria

Frees, Dorte, Savijoki, Kirsi, Varmanen, Pekka, Ingmer, Hanne·2007·Molecular Microbiology

Abstract

Summary: Clp proteolytic complexes consisting of a proteolytic core flanked by Clp ATPases are widely conserved in bacteria, and their biological roles have received considerable interest. In particular, mutants in the clp genes in the low‐GC‐content Gram‐positive phyla Bacillales and Lactobacillales display a diverse range of phenotypic changes including general stress sensitivity, aberrant cell morphology, failure to initiate developmental programs, and for pathogens, severely attenuated virulence. Extensive research dedicated to unravelling the molecular mechanisms underlying these complex phenotypes has led to fascinating new insights that will be covered by this review. First, Clp ATPases and ClpP‐containing proteolytic complexes play indispensable roles in cellular protein quality control systems by refolding or degrading damaged proteins in both stressed and non‐stressed cells. Secondly, ClpP proteases and the chaperone activity of Clp ATPases are important for controlling stability and activity of central transcriptional regulators, thereby exerting tremendous impact on cell physiology. Targets include major stress regulators like Spx (oxidative stress), the antisigma factor RsiW (alkaline stress) and HdiR (DNA damage) in addition to regulators of developmental programs like ComK (competence development), σ H and Sda (sporulation). Thus, Clp proteins are central in co‐ordinating developmental decisions and stress response in low GC Gram‐positive bacteria.

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Crossref · 10.1111/j.1365-2958.2007.05598.x

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Authors
Frees, D., Savijoki, K., Varmanen, P., & Ingmer, H.
Affiliations
  • University of Copenhagen (DK)
  • University of Helsinki (FI)
Corresponding author
Ingmer, Hanne
Venue
Molecular Microbiology
Publisher
Wiley
Published
2007-01-15
Volume
63
Issue
5
Pages
1285-1295
ISSN
  • 0950-382X (ISSN-L)
  • 1365-2958
OpenAlex
W2165412123
Cited by
288
References
82
Citations by year
2026: 11 · 2025: 10 · 2024: 9 · 2023: 16 · 2022: 11 · 2021: 13 · 2020: 17 · 2019: 16 · 2018: 13 · 2017: 13 · 2016: 16 · 2015: 6 · 2014: 15 · 2013: 25 · 2012: 21
FWCI
1.38
Type
journal article
Language
en
Open access
closed
Locations
  • Molecular Microbiology (publishedVersion)
  • PubMed (publishedVersion)
  • Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Keywords
Bacillales, Lactobacillales, protein quality control, protein refolding, protein degradation, chaperone activity, transcription factors, stress response, oxidative stress, alkaline stress, DNA damage, competence development, sporulation, virulence attenuation, cell morphology
MeSH terms
Adenosine Triphosphatases, Bacterial Proteins, Gram-Positive Bacteria, Endopeptidase Clp

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