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ClpAP proteolysis does not require rotation of the ClpA unfoldase relative to ClpP
- Source :
- eLife, Vol 9 (2020), eLife
- Publication Year :
- 2020
- Publisher :
- Cold Spring Harbor Laboratory, 2020.
-
Abstract
- AAA+ proteases, which perform regulated protein degradation in all kingdoms of life, consist of a hexameric AAA+ unfoldase/translocase in complex with a self-compartmentalized peptidase. Based on asymmetric features of cryo-EM structures and a sequential hand-over-hand model of substrate translocation, recent publications have proposed that the AAA+ unfoldases ClpA and ClpX must rotate with respect to their partner peptidase ClpP to allow function. Here, we test this model by covalently crosslinking ClpA to ClpP to prevent rotation. We find that crosslinked ClpAP omplexes unfold, translocate, and degrade protein substrates, albeit modestly slower han uncrosslinked enzyme controls. Rotation of ClpA with respect to ClpP therefore is ot required for ClpAP protease activity, although some flexibility in how the AAA+ ring ocks on ClpP may be necessary for optimal function.
- Subjects :
- Models, Molecular
Protein Folding
Proteases
Protein Conformation
QH301-705.5
Structural Biology and Molecular Biophysics
Science
medicine.medical_treatment
Proteolysis
Short Report
aaa+ protease
ClpXP
macromolecular substances
Protein degradation
General Biochemistry, Genetics and Molecular Biology
Biochemistry and Chemical Biology
Escherichia coli
medicine
Translocase
Biology (General)
ClpAP
Protease
General Immunology and Microbiology
biology
medicine.diagnostic_test
Chemistry
Escherichia coli Proteins
General Neuroscience
E. coli
Endopeptidase Clp
General Medicine
AAA proteins
Cross-Linking Reagents
Structural biology
aaa+ atpase
biology.protein
Biophysics
Medicine
Subjects
Details
- Database :
- OpenAIRE
- Journal :
- eLife, Vol 9 (2020), eLife
- Accession number :
- edsair.doi.dedup.....b59fd90729d10bcf2541920811ebb6a8
- Full Text :
- https://doi.org/10.1101/2020.07.26.221812