Dataset Information

Effect of depletion of clpP2, clpX and clpC1 genes on whole cell proteome profile of Mycobacterium tuberculosis H37Rv

ABSTRACT: Global protein alteration in Mycobacterium tuberculosis H37 RV ( Mtb-H37RV) having depletion of Clpx ,Clp2 and ClpC1 were accessed using 4 plex iTRAQ label.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Mycobacterium Tuberculosis Mycobacterium Tuberculosis H37rv

SUBMITTER: Nisheeth Agarwal

LAB HEAD: Nisheeth Agarwal

PROVIDER: PXD013589 | Pride | 2020-05-14

REPOSITORIES: Pride

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Publications

The unfoldase ClpC1 of <i>Mycobacterium tuberculosis</i> regulates the expression of a distinct subset of proteins having intrinsically disordered termini.

Lunge Ajitesh A Gupta Radhika R Choudhary Eira E Agarwal Nisheeth N

The Journal of biological chemistry 20200514 28

The human pathogen <i>Mycobacterium tuberculosis</i> (Mtb) harbors a well-orchestrated Clp (caseinolytic protease) proteolytic machinery consisting of two oligomeric segments, a barrel-shaped heterotetradecameric protease core comprising the ClpP1 and ClpP2 subunits, and hexameric ring-like ATP-dependent unfoldases composed of ClpX or ClpC1. The roles of the ClpP1P2 protease subunits are well-established in Mtb, but the potential roles of the associated unfoldases, such as ClpC1, remain elusive. ...[more]

PMID: 32409584

Similar Datasets

Project description:In chloroplasts, homeostasis of the proteome maintained by protein synthesis, importation, and degradation is critical to the development of chloroplasts. The caseinolytic protease complex component CLPC1, a member of the HSP100 family of chaperones, not only facilitates the translocation of pre-proteins into chloroplasts, but also mediates protein degradation via its associated caseinolytic protease complex (CLPPs). Although CLPC1 has been shown to affect the abundance of some chloroplast proteins, its overall functions and coordination with other protease systems in maintaining proteome homeostasis have not been fully elucidated. Its possible roles in gene expression are also unclear. Here we used the iTRAQ technique to profile the chloroplast proteomes of the clpc1 mutant and its various complementation lines. Whereas proteins involved in photosynthesis were found to be dramatically decreased in the clcp1 mutant, many involved in chloroplast transcription and translation were increased. Expression of the full-length CLPC1 protein, but not of the N-terminal truncated form (ΔN), in clpc1 restored the level of most of these proteins to that of the wild type. Interestingly, the ΔN complementation line could also restore certain proteins to the wild type level. We found that nearly half of previously suggested candidate substrates of the CLPS1, another CLPP component, were mis-regulated in clpc1, indicating that CLPC1 greatly affects CLPS1 targets. We provide the first experimental evidence to show that CLPC1 profoundly affects gene transcription in chloroplasts. Sense transcripts of many chloroplast genes are up-regulated whereas antisense transcripts down-regulated in the clpc1 mutant. We propose that this altered transcript landscape is a result of the transcription and degradation dynamics conditioned by the changed proteomic profile in the mutant. Our study reveals that CLPC1 and likely the CLPP proteasome complex have a greater than previously recognized role in coordinating and maintaining the proteome and transcriptome homeostasis in chloroplasts.

			Action	DRS
	CLPSET1.1.wiff	Wiff
	CLPSET1.1.wiff.scan	Wiff
	CLPSET1.2.wiff	Wiff
	CLPSET1.2.wiff.scan	Wiff
	CLPSET1.3.wiff	Wiff