Clp protease family
| CLP_protease | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of the clpp protease catalytic domain from plasmodium falciparum | |||||||||
| Identifiers | |||||||||
| Symbol | CLP_protease | ||||||||
| Pfam | PF00574 | ||||||||
| Pfam clan | CL0127 | ||||||||
| InterPro | IPR001907 | ||||||||
| PROSITE | PDOC00358 | ||||||||
| MEROPS | S14 | ||||||||
| SCOP2 | 1tyf / SCOPe / SUPFAM | ||||||||
| CDD | cd00394 | ||||||||
| |||||||||
In molecular biology, the CLP protease family is a family of serine peptidases belong to the MEROPS peptidase family S14 (ClpP endopeptidase family, clan SK). ClpP is an ATP-dependent protease that cleaves a number of proteins, such as casein and albumin.[1] It exists as a heterodimer of ATP-binding regulatory A and catalytic P subunits, both of which are required for effective levels of protease activity in the presence of ATP,[1] although the P subunit alone does possess some catalytic activity.
Proteases highly similar to ClpP have been found to be encoded in the genome of bacteria, in the mitochondria of metazoa, some viruses and in the chloroplast of plants. A number of the proteins in this family are classified as non-peptidase homologues as they have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for catalytic activity.
Mutations in mitochondrial CLPP are associated with Perrault syndrome[2][3][4][5] and cause a variety of molecular defects, from the loss of ATPase docking, to the activation or inhibition of peptidase activity.[3][6]
See also
[edit]References
[edit]- ^ a b Maurizi MR, Clark WP, Katayama Y, Rudikoff S, Pumphrey J, Bowers B, Gottesman S (July 1990). "Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli". The Journal of Biological Chemistry. 265 (21): 12536–45. doi:10.1016/S0021-9258(19)38378-4. PMID 2197275.
- ^ Newman, W. G.; Friedman, T. B.; Conway, G. S.; Demain LAM; Adam, M. P.; Ardinger, H. H.; Pagon, R. A.; Wallace, S. E.; Bean LJH; Stephens, K.; Amemiya, A. (1993). Adam, Margaret P.; Ardinger, Holly H.; Pagon, Roberta A.; Wallace, Stephanie E. (eds.). "Perrault Syndrome". GeneReviews. Seattle (WA): University of Washington, Seattle. PMID 25254289. Retrieved 2020-11-18.
- ^ a b Jenkinson EM, Rehman AU, Walsh T, Clayton-Smith J, Lee K, Morell RJ, et al. (April 2013). "Perrault syndrome is caused by recessive mutations in CLPP, encoding a mitochondrial ATP-dependent chambered protease". American Journal of Human Genetics. 92 (4): 605–13. doi:10.1016/j.ajhg.2013.02.013. PMC 3617381. PMID 23541340.
- ^ Ahmed S, Jelani M, Alrayes N, Mohamoud HS, Almramhi MM, Anshasi W, et al. (June 2015). "Exome analysis identified a novel missense mutation in the CLPP gene in a consanguineous Saudi family expanding the clinical spectrum of Perrault Syndrome type-3". Journal of the Neurological Sciences. 353 (1–2): 149–54. doi:10.1016/j.jns.2015.04.038. PMID 25956234. S2CID 6053528.
- ^ Dursun F, Mohamoud HS, Karim N, Naeem M, Jelani M, Kırmızıbekmez H (December 2016). "A Novel Missense Mutation in the CLPP Gene Causing Perrault Syndrome Type 3 in a Turkish Family". Journal of Clinical Research in Pediatric Endocrinology. 8 (4): 472–477. doi:10.4274/jcrpe.2717. PMC 5198008. PMID 27087618.
- ^ Brodie EJ, Zhan H, Saiyed T, Truscott KN, Dougan DA (August 2018). "Perrault syndrome type 3 caused by diverse molecular defects in CLPP". Scientific Reports. 8 (1): 12862. Bibcode:2018NatSR...812862B. doi:10.1038/s41598-018-30311-1. PMC 6110781. PMID 30150665.
External links
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