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Results 1 - 10 of 18 > >>
EC Number
General Information
Commentary
Reference
malfunction
a point mutation from G to A at nucleotide 2317 of ClpC1 on chromosome V of Arabidopsis is responsible for the irm1 phenotype (typical Fe-deficiency chlorosis)
malfunction
both FlhD and FlhC regulator proteins accumulate markedly following ClpXP depletion, and their half-lives are significantly longer in the mutant cells
malfunction
ClpP1 is essential for viability. The gene can only be deleted from the chromosome when a second functional copy is provided. Over-expression of clpP1 has no effect on growth in aerobic culture or viability under anaerobic conditions or during nutrient starvation; clpP2 over-expression is toxic
malfunction
deletion of clpX and clpP suppresses temperature-sensitive filamentation of cells carrying the ftsZ84 allele and reduces FtsZ84 degradation, consistent with ClpXP (two-component protease composed of ClpX and ClpP) playing a role in modulating the level of FtsZ (a tubulin-like protein); in a division-defective strain, DELTAminC, the additional deletion of clpX or clpP delays cell division and exacerbates filamentation
malfunction
in a DELTAclpP strain, 288 genes show significant changes in relative transcript amounts as compared with the parent. Similarly, 242 genes are differentially expressed by a DELTAclpX strain. Several genes associated with cell growth are down-regulated in both mutants, consistent with the slow-growth phenotype of the DELTAclp strains. Among the up-regulated genes are those encoding enzymes required for the biosynthesis of intracellular polysaccharides and malolactic fermentation. Expression of several genes known or predicted to be involved in competence and mutacin production are down-regulated in the DELTAclp strains
physiological function
a mutant strain lacking the N-terminal domain of ClpX is not viable
physiological function
accessory proteins ClpT1 and ClpT2 regulate the assembly of the Clp proteolytic core in vascular plants
physiological function
adaptor protein MecA specifically interacts with both central competence regulator sigmax and protease ClpC, suggesting the formation of a ternary sigmaX-MecA-ClpC complex. MecA ultimately targets sigmaX for its degradation by the ClpCP protease in an ATP-dependent manner. A short sequence of 18 amino acids in the N-terminal domain of sigmaX is essential for the interaction with MecA and subsequent sigmaX degradation. Increased transformability of a MecA-deficient strain in the presence of subinducing SigX-inducing peptide concentrations suggests that the MecA-ClpCP proteolytic complex acts as an additional locking device to prevent competence under inappropriate conditions
physiological function
Azotobacter vinelandii carries a duplicated copy of the ATPase component of the ubiquitous ClpXP protease (ClpX2), which is induced under nitrogen fixing conditions. Inactivation of clpX2 results in the accumulation of NifB and NifEN and a defect in diazotrophic growth, especially when iron is in short supply
physiological function
both protein and small-molecule activators of ClpP allosterically control the ClpP barrel conformation. Acyldepsipeptides in addition to opening the axial pore directly stimulate ClpP activity through cooperative binding. ClpP activation thus reaches beyond active site accessibility and also involves conformational control of the catalytic residues. Substoichiometric amounts of acyldepsipeptide potently prevent binding of ClpX to ClpP and, at the same time, partially inhibit ClpP through conformational perturbance. The hydrophobic binding pocket is a major conformational regulatory site with implications for both ClpXP proteolysis and acyldepsipeptide -based anti-bacterial activity
Results 1 - 10 of 18 > >>