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...
Main Authors: | Wojtyra, U. A., Houry, Walid A., Thibault, Guillaume, Tuite, Ashleigh |
---|---|
Other Authors: | School of Biological Sciences |
Format: | Journal Article |
Language: | English |
Published: |
2013
|
Subjects: | |
Online Access: | https://hdl.handle.net/10356/100398 http://hdl.handle.net/10220/17900 |
Similar Items
-
Mechanism and consequences of Mu transpososome remodeling by the ClpX chaperone
by: Burton, Briana M. (Briana Marie), 1977-
Published: (2005) -
Stimulation of transcript elongation requires both the zinc finger and RNA polymerase II binding domains of human TFIIS
by: Agarwal, Kan, et al.
Published: (2012) -
Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
by: Harlan, John E., et al.
Published: (2012) -
The zinc-binding domain of mammalian prolyl-tRNA synthetase is indispensable for catalytic activity and organism viability
by: Kommireddy Vasu, et al.
Published: (2021-03-01) -
Control of substrate gating and translocation into ClpP by channel residues and ClpX binding
by: Lee, Mary E., et al.
Published: (2012)