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• W2488156724 startingPage "798" @default.
• W2488156724 abstract "This chapter presents an overview of the structural chemistry and the biological aspects of mitochondrial m- and i-AAA proteases. The mitochondrial m- and i-AAA proteases were originally discovered in the budding yeast Saccharomyces cerevisiae. Yme1p, Yta10p and Yta12p form a subfamily of the AAA family of proteins. All AAA family members exhibit a highly conserved domain of 300 amino acids containing specialized forms of ATPase A and B boxes, and a highly homologous region of 63 amino acid residues, referred to as the DEXD domain. The mitochondrial AAA proteases from all sources share extensive sequence similarities with each other and with the FtsH protein of E. coli. All of these proteins are similar in size and are integral membrane proteins, and contain a sequence motif (HEXXH) characteristic of metallopeptidases in clans MA and MB. The m-AAA protease complex, composed of Ytal0p and Ytal2p, has an important chaperone function in the assembly of mitochondrial inner-membrane protein complexes. This function is dependent upon the inherent ATPase activity of Yta10p and Yta12p." @default.
• W2488156724 created "2016-08-23" @default.
• W2488156724 creator A5076791930 @default.
• W2488156724 creator A5082884818 @default.
• W2488156724 date "2004-01-01" @default.
• W2488156724 modified "2023-09-23" @default.
• W2488156724 title "Mitochondrial m- and i-AAA proteases" @default.
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• W2488156724 doi "https://doi.org/10.1016/b978-0-12-079611-3.50243-3" @default.
• W2488156724 hasPublicationYear "2004" @default.
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