ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial

Definition:

ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex. Can perform chaperone functions in the absence of CLPP. Enhances the DNA-binding activity of TFAM and is required for maintaining a normal mitochondrial nucleoid structure. ATP-dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis. Important for efficient erythropoiesis through up-regulation of heme biosynthesis.

References:

[1]. Julia R Kardon, et al. Mitochondrial ClpX Activates a Key Enzyme for Heme Biosynthesis and Erythropoiesis. Cell. 2015 May 7;161(4):858-67. [Content Brief]

[2]. Katsumi Kasashima, et al. Maintenance of mitochondrial genome distribution by mitochondrial AAA+ protein ClpX. Exp Cell Res. 2012 Nov 1;318(18):2335-43. [Content Brief]

[3]. Sung Gyun Kang, et al. Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP. J Biol Chem. 2002 Jun 7;277(23):21095-102. [Content Brief]

[4]. Bradley R Lowth, et al. Substrate recognition and processing by a Walker B mutant of the human mitochondrial AAA+ protein CLPX. J Struct Biol. 2012 Aug;179(2):193-201. [Content Brief]

[5]. Yvette Y Yien, et al. Mutation in human CLPX elevates levels of δ- aminolevulinate synthase and protoporphyrin IX to promote erythropoietic protoporphyria. Proc Natl Acad Sci U S A. 2017 Sep 19;114(38):E8045-E8052. [Content Brief]

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