Disease relevance of clpP

• The genes that encode the subunits of the Clp protease of Escherichia coli, clpA and clpP, appear to be regulated differently from each other [1].
• The nucleotide sequence of the Bacillus subtilis clpP gene was determined [2].
• Distinct clpP genes control specific adaptive responses in Bacillus thuringiensis [3].
• We have cloned a clpP gene, designated clpP1, from the cyanobacterium Synechococcus sp. PCC 7942 [4].

High impact information on clpP

• The clpP gene is at 10 min on the E. coli map, close to that for the ATP-dependent Lon protease of E. coli and far from the gene for clpA [5].
• The DNA sequence of the clpP gene predicts a protein of 207 amino acids (Mr 21,679), which is in close agreement with the size determined by sodium dodecyl sulfate-gel electrophoresis of purified Clp P [5].
• Insertion mutations in clpP have been isolated and transferred to the chromosome; strains devoid of Clp P are viable in the presence or absence of Lon protease [5].
• This turnover is dependent on the clpP and clpX genes [6].
• Increased levels of MecA in the absence of ClpP are at least partly responsible for the observed pleiotropic phenotype of the delta clpP mutant [2].

Biological context of clpP

• For example, in the clpP and clpA mutant cultures, the Dps protein, the WrbA protein, and the periplasmic lysine-arginine-ornithine binding protein ArgT did not display the induction typical for late-stationary-phase wild-type cells [7].
• An analysis of the degradation kinetics shows that Rep is a target of two protease systems: inactivation of either the clpP or lon gene results in a stabilization of Rep. Such a reaction scheme explains the counterintuitive observation that derepression is correlated with high repressor concentration [8].
• In this study, we further investigated the underlying mechanism of virulence attenuation by the clpP mutation [9].
• Nucleotide sequence analysis of the Streptococcus salivarius clpP locus revealed potential binding sites for both the CtsR and HrcA repressors [10].
• Based on the amino acid sequences of the Bacillus subtilis clpC and clpP genes, we identified one clpC gene and two clpP genes (designated clpP1 and clpP2) in Bacillus thuringiensis [3].

Anatomical context of clpP

• In addition, the clpP mutant was defective in colonization of the nasopharynx and survival in the lungs of mice after intranasal challenge [9].

Associations of clpP with chemical compounds

• Lethality fixation did progress when protein synthesis was restricted and the cells were incubated in the presence of puromycin or were either clpP or clpX defective [11].

References