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ClpP: A distinctive family of cylindrical energy‐dependent serine proteases

2007; Wiley; Volume: 581; Issue: 19 Linguagem: Inglês

10.1016/j.febslet.2007.04.076

1873-3468

Angela Yeou Hsiung Yu, Walid A. Houry,

Bacterial Genetics and Biotechnology

Processes maintaining protein homeostasis in the cell are governed by the activities of molecular chaperones that mainly assist in the folding of polypeptide chains and by a large class of proteases that regulate protein levels through degradation. ClpP proteases define a distinctive family of cylindrical, energy-dependent serine proteases that are highly conserved throughout bacteria and eukaryota. They typically interact with ATP-dependent AAA+ chaperones that bind and unfold target substrates and then translocate them into ClpP for degradation. Structural and functional studies have provided a detailed view of the mechanism of function of this class of proteases.