Journal
GENES & DEVELOPMENT
Volume 18, Issue 4, Pages 369-374Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.1170304
Keywords
AAA ATPase; peptide binding; protein unfolding; protein translocation
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Funding
- NIAID NIH HHS [AI-16892, R01 AI016892] Funding Source: Medline
- NIGMS NIH HHS [R01 GM049224, R01 GM049224-11] Funding Source: Medline
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ClpX binds substrates bearing specific classes of peptide signals, denatures these proteins, and translocates them through a central pore into ClpP for degradation. ClpX with the V154F pore mutation is severely defective in binding substrates bearing C-motif I degradation signals and is also impaired in a subsequent step of substrate engagement. In contrast, this mutant efficiently processes substrates with other classes of recognition signals both in vitro and in vivo. These results demonstrate that the ClpX pore functions in the recognition and catalytic engagement of specific substrates, and that ClpX recognizes different substrate classes in at least two distinct fashions.
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