caseinolytic mitochondrial matrix peptidase proteolytic subunit
Dernière mise à jour 18 Aug 2020
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La CLPP gene provides instructions for making the ClpP subunit protein. Multiple copies of this protein interact with each other to form a barrel-shaped chamber known as the ClpP complex. This complex is one of two parts of the ClpXP protease, which breaks down abnormally folded proteins. The other part of the ClpXP protease, called the ClpX complex, unfolds the abnormal proteins and feeds them into the chamber formed by the ClpP complex, where they are broken down into small fragments.
Normal function
La CLPP gene provides instructions for making the ClpP subunit protein. Multiple copies of this protein interact with each other to form a barrel-shaped chamber known as the ClpP complex. This complex is one of two parts of the ClpXP protease, which breaks down abnormally folded proteins. The other part of the ClpXP protease, called the ClpX complex, unfolds the abnormal proteins and feeds them into the chamber formed by the ClpP complex, where they are broken down into small fragments.
The ClpP complex is found in structures in the cell called mitochondria, which are the energy-producing centers of cells.
Conditions referring to this gene or chromosome
Other names
ATP-dependent Clp protease proteolytic subunit, mitochondrial
ATP-dependent protease ClpAP, proteolytic subunit, human
ClpP caseinolytic peptidase ATP-dependent, proteolytic subunit
ClpP caseinolytic protease, ATP-dependent, proteolytic subunit homolog
endopeptidase Clp
PRLTS3
putative ATP-dependent Clp protease proteolytic subunit, mitochondrial
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Lectures complémentaires et références
- caseinolytic mitochondrial matrix peptidase proteolytic subunit; MedlinePlus, National Library of Medicine.
- Baker TA, Sauer RT. ClpXP, an ATP-powered unfolding and protein-degradation machine. Biochim Biophys Acta. 2012 Jan;1823(1):15-28. doi: 10.1016/j.bbamcr.2011.06.007. Epub 2011 Jun 27.
- Jenkinson EM, Rehman AU, Walsh T, Clayton-Smith J, Lee K, Morell RJ, Drummond MC, Khan SN, Naeem MA, Rauf B, Billington N, Schultz JM, Urquhart JE, Lee MK, Berry A, Hanley NA, Mehta S, Cilliers D, Clayton PE, Kingston H, Smith MJ, Warner TT; University of Washington Center for Mendelian Genomics; Black GC, Trump D, Davis JR, Ahmad W, Leal SM, Riazuddin S, King MC, Friedman TB, Newman WG. Perrault syndrome is caused by recessive mutations in CLPP, encoding a mitochondrial ATP-dependent chambered protease. Am J Hum Genet. 2013 Apr 4;92(4):605-13. doi: 10.1016/j.ajhg.2013.02.013. Epub 2013 Mar 28.
- Kang SG, Dimitrova MN, Ortega J, Ginsburg A, Maurizi MR. Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX. J Biol Chem. 2005 Oct 21;280(42):35424-32. doi: 10.1074/jbc.M507240200. Epub 2005 Aug 22.
- Yu AY, Houry WA. ClpP: a distinctive family of cylindrical energy-dependent serine proteases. FEBS Lett. 2007 Jul 31;581(19):3749-57. doi: 10.1016/j.febslet.2007.04.076. Epub 2007 May 8.
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