OpenSSL SSL_connect: Connection reset by peer in connection to v2.sherpa.ac.uk:443 PuSH - Publication Server of Helmholtz Zentrum München: Molecular transformers in the cell: Lessons learned from the DegP protease-chaperone.

PuSH - Publication Server of Helmholtz Zentrum München

Sawa, J.* ; Heuck, A. ; Ehrmann, M.* ; Clausen, T.*

Molecular transformers in the cell: Lessons learned from the DegP protease-chaperone.

Curr. Opin. Struct. Biol. 20, 253-258 (2010)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
Structure-function analysis of DegP revealed a novel mechanism for protease and chaperone regulation. Binding of unfolded proteins induces the oligomer reassembly from the resting hexamer (DegP6) into the functional protease-chaperone DegP12/24. The newly formed cage exhibits the characteristics of a proteolytic folding chamber, shredding those proteins that are severely misfolded while stabilizing and protecting proteins present in their native state. Isolation of native DegP complexes with folded outer membrane proteins (OMPs) highlights the importance of DegP in OMP biogenesis. The encapsulated OMP beta-barrel is significantly stabilized in the hydrophobic chamber of DegP12/24 and thus DegP seems to employ a reciprocal mechanism to those chaperones assisting the folding of water soluble proteins via polar interactions. In addition, we discuss in this review similarities to other complex proteolytic machines that, like DegP, are under control of a substrate-induced or stress-induced oligomer conversion.
Altmetric
Additional Metrics?
[➜Log in]
Edit extra informations Login
Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords outer-membrane proteins; escherichia-coli; quality-control; substrate recognition; periplasmic protein; regulatory particle; bacterial protein; crystal-structure; assembly pathway; structural basis
ISSN (print) / ISBN 0959-440X
e-ISSN 1879-033X
Journal Current Opinion in Structural Biology
Quellenangaben Volume: 20, Issue: 2, Pages: 253-258 Article Number: , Supplement: ,
Publisher Elsevier
Publishing Place London
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)