The N-terminal zinc binding domain of ClpX is a dimerization domain that modulates the chaperone function
Clp ATPases are unique chaperones that promote protein unfolding and subsequent degradation by proteases. The mechanism by which this occurs is poorly understood. Here we demonstrate that the N-terminal domain of ClpX is a C4-type zinc binding domain (ZBD) involved in substrate recognition. ZBD...
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| Main Authors: | , , , |
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| Other Authors: | |
| Format: | Article |
| Language: | English |
| Published: |
2013
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| Subjects: | |
| Online Access: | https://hdl.handle.net/10356/100398 http://hdl.handle.net/10220/17900 |
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| Institution: | Nanyang Technological University |
| Language: | English |
| Summary: | Clp ATPases are unique chaperones that promote protein
unfolding and subsequent degradation by proteases.
The mechanism by which this occurs is poorly
understood. Here we demonstrate that the N-terminal
domain of ClpX is a C4-type zinc binding domain (ZBD)
involved in substrate recognition. ZBD forms a very stable
dimer that is essential for promoting the degradation
of some typical ClpXP substrates such as _O and
MuA but not GFP-SsrA. Furthermore, experiments indicate
that ZBD contains a primary binding site for the _O
substrate and for the cofactor SspB. Removal of ZBD
from the ClpX sequence renders the ATPase activity of
ClpX largely insensitive to the presence of ClpP, substrates,
or the SspB cofactor. All these results indicate
that ZBD plays an important role in the ClpX mechanism
of function and that ATP binding and/or hydrolysis
drives a conformational change in ClpX involving ZBD. |
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