PMID:18179597
| Citation |
Marshall-Batty, KR and Nakai, H (2008) Trans-targeting of protease substrates by conformationally activating a regulable ClpX-recognition motif. Mol. Microbiol. 67:920-33 |
|---|---|
| Abstract |
Conversion of bacteriophage Mu repressor to ClpXP-sensitive form correlates with induced local flexibility at the ClpX recognition motif located at the C-terminal end. Changing the C-terminal valine to an alanine (RepV196A) caused the degradation tag to be constitutively active like that of mutant repressors called Vir, which have a dominant ClpXP-sensitive conformation. However, unlike Vir, RepV196A was unable to convert wild-type repressor (Rep) to the ClpXP-sensitive form. In mixtures with Rep, only RepV196A was rapidly degraded by ClpXP. Unlike Rep, RepV196A was ClpXP sensitive without induced C-terminal flexibility. And unlike adaptor proteins that tether and deliver substrates to ClpX for trans-targeting, Vir promoted rapid degradation of Rep by ClpX deleted for the tethering site that binds adaptor proteins. Therefore, Rep's ClpX recognition motif has regulable properties, allowing an alternative trans-targeting mechanism in which an inactive degradation tag is turned on by induced conformational changes. |
| Links |
PubMed Online version:10.1111/j.1365-2958.2007.06099.x |
| Keywords |
Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Amino Acid Motifs; Bacteriophage mu/genetics; Bacteriophage mu/metabolism; Endopeptidase Clp/chemistry; Endopeptidase Clp/genetics; Endopeptidase Clp/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Molecular Chaperones/chemistry; Molecular Chaperones/genetics; Molecular Chaperones/metabolism; Mutation; Repressor Proteins/chemistry; Repressor Proteins/metabolism; Viral Proteins/genetics; Viral Proteins/metabolism |
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