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ClpP: A distinctive family of cylindrical energy‐dependent serine proteases
Author(s) -
Yu Angela Yeou Hsiung,
Houry Walid A.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.04.076
Subject(s) - proteases , serine , protein folding , biochemistry , microbiology and biotechnology , function (biology) , protein family , biology , mechanism (biology) , chemistry , enzyme , gene , philosophy , epistemology
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.