ArticleJournal of bacteriology2012
DnaK dependence of the mycobacterial stress-responsive regulator HspR is mediated through its hydrophobic C-terminal tail.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
- Expanding the CarD interaction network: CrsL is a novel transcription regulator in actinobacteria.Nucleic acids research · 2025Article
- Age-Dependent Pleomorphism inMicroorganisms · 2025Article
- Structure of the M. tuberculosis DnaK-GrpE complex reveals how key DnaK roles are controlled.Nature communications · 2024Article
- The Functionality of IbpA fromInternational journal of molecular sciences · 2023Article
- ATP-independent substrate recruitment to proteasomal degradation in mycobacteria.Life science alliance · 2023Article
- Purification and Characterization of Authentic 30S Ribosomal Precursors Induced by Heat Shock.International journal of molecular sciences · 2023Article
- An immunoinformatics approach to design a multi-epitope vaccine against Mycobacterium tuberculosis exploiting secreted exosome proteins.Scientific reports · 2021Article
- The Transcriptional Regulatory Network ofMicroorganisms · 2021Review
- Transcriptional Response ofFrontiers in microbiology · 2021Article
- Survival in Hostile Conditions: Pupylation and the Proteasome in Actinobacterial Stress Response Pathways.Frontiers in molecular biosciences · 2021Review
- Functioning of Mycobacterial Heat Shock Repressors Requires the Master Virulence Regulator PhoP.Journal of bacteriology · 2019Article
- Comparison of immunogenicity and vaccine efficacy between heat-shock proteins, HSP70 and GrpE, in the DnaK operon of Mycobacterium tuberculosis.Scientific reports · 2018Article
- Targeting the Proteostasis Network for Mycobacterial Drug Discovery.ACS infectious diseases · 2018Review
- Article
- Loss-of-Function Mutations in HspR Rescue the Growth Defect of a Mycobacterium tuberculosis Proteasome Accessory Factor E (Journal of bacteriology · 2017Article
- Bacterial Proteasomes: Mechanistic and Functional Insights.Microbiology and molecular biology reviews : MMBR · 2017Review
- Reconstitution of a Mycobacterium tuberculosis proteostasis network highlights essential cofactor interactions with chaperone DnaK.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Chaperone addiction of toxin-antitoxin systems.Nature communications · 2016Article
- An adenosine triphosphate-independent proteasome activator contributes to the virulence of Mycobacterium tuberculosis.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Drug-resistant tuberculosis can be predicted by Mycobacterial interspersed repetitive unit locus.Frontiers in microbiology · 2015Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
HspR is a repressor known to control expression of heat shock operons in a number of Eubacteria. In mycobacteria and in several other actinobacteria, this protein is synthesized from the dnaKJE-hspR operon. Previous investigations revealed that HspR binds to the operon promoter, thereby controlling its expression in an autoregulatory manner. DnaK, which is a product of the same operon, further aids this autoregulatory process by stimulating the operator binding activity of HspR. The molecular mechanism by which DnaK assists HspR in executing its function is not clearly understood. In this study, it has been shown that DnaK can augment DNA binding activity of HspR by two mechanisms: (i) DnaK can restore the activity of completely denatured HspR by forming a complex with it, and (ii) DnaK can prevent thermal instability of HspR renatured by other means. Unlike the first mechanism, the latter function does not involve complex formation. The C-terminal hydrophobic tail of HspR was found to play a significant role in determining its thermal stability and DnaK dependence properties. A deletion mutant in which this region is removed does not respond to thermal stress and functions independent of DnaK. The hydrophobic C-terminal tails of HspRs of Mycobacterium tuberculosis and related Actinomycetales therefore may have evolved to make these HspRs more sensitive to thermal stress and, at the same time, subject to regulation by DnaK.
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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.