ArticleMolecular genetics and genomics : MGG2003
The ATPase ClpX is conditionally involved in the morphological differentiation of Streptomyces lividans.
Article in Molecular genetics and genomics : MGG, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- ONC201 Suppresses Neuroblastoma Growth by Interrupting Mitochondrial Function and Reactivating Nuclear ATRX Expression While Decreasing MYCN.International journal of molecular sciences · 2023Article
- Antibiotic Acyldepsipeptides Stimulate themBio · 2022Article
- Article
- Insights to the Assembly of a Functionally Active Leptospiral ClpP1P2 Protease Complex along with Its ATPase Chaperone ClpX.ACS omega · 2019Article
- Bacterial proteases, untapped antimicrobial drug targets.The Journal of antibiotics · 2017Review
- Signals and regulators that govern Streptomyces development.FEMS microbiology reviews · 2012Review
- spr1630 is responsible for the lethality of clpX mutations in Streptococcus pneumoniae.Journal of bacteriology · 2009Article
- The SmpB-tmRNA tagging system plays important roles in Streptomyces coelicolor growth and development.PloS one · 2009Article
- The ClgR protein regulates transcription of the clpP operon in Bifidobacterium breve UCC 2003.Journal of bacteriology · 2005Article
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Authors and funding
2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
ATP-dependent proteases of the ClpP type are widespread in eubacteria. These proteolytic complexes are composed of a proteolytic subunit and an ATPase subunit. They are involved in the degradation of denatured proteins, but also play a role in specific regulatory pathways. In Streptomyces lividans strains which lack the proteolytic subunit ClpP1, cell cycle progression has been shown to be blocked at early stages of growth. In this study, we examined the role of the ATPase subunit ClpX, a possible partner of the products of the clpP1 operon. A clpX mutant was obtained and it was shown that its growth was impaired only on acidic medium. Thus, the clpX phenotype differs from the clpP1 phenotype, indicating that these two components have only partially overlapping roles. We also analyzed the expression of clpX. Although clpX expression is increased under heat-shock conditions in many bacteria, we found that this is not the case in S. lividans.
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