Abstract：
:ClpXP is a protein machine composed of the ClpX ATPase, a member of the Clp/Hsp100 family of remodeling enzymes, and the ClpP peptidase. Here, ClpX and ClpXP are shown to catalyze denaturation of GFP modified with an ssrA degradation tag. ClpX translocates this denatured protein into the proteolytic chamber of ClpP and, when proteolysis is blocked, also catalyzes release of denatured GFP-ssrA from ClpP in a reaction that requires ATP and additional substrate. Kinetic experiments reveal that multiple reaction steps require collaboration between ClpX and ClpP and that denaturation is the rate-determining step in degradation. These insights into the mechanism of ClpXP explain how it executes efficient degradation in a manner that is highly specific for tagged proteins, irrespective of their intrinsic stabilities.
journal_name
Mol Celljournal_title
Molecular cellauthors
Kim YI,Burton RE,Burton BM,Sauer RT,Baker TAdoi
10.1016/s1097-2765(00)80243-9subject
Has Abstractpub_date
2000-04-01 00:00:00pages
639-48issue
4eissn
1097-2765issn
1097-4164pii
S1097-2765(00)80243-9journal_volume
5pub_type
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