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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 möglich sobald Postprint bei der ZB eingereicht worden ist.
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.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter outer-membrane proteins; escherichia-coli; quality-control; substrate recognition; periplasmic protein; regulatory particle; bacterial protein; crystal-structure; assembly pathway; structural basis
Sprache englisch
Veröffentlichungsjahr 2010
HGF-Berichtsjahr 2010
ISSN (print) / ISBN 0959-440X
e-ISSN 1879-033X
Zeitschrift Current Opinion in Structural Biology
Quellenangaben Band: 20, Heft: 2, Seiten: 253-258 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort London
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)
PSP-Element(e) G-551400-001
PubMed ID 20188538
DOI 10.1016/j.sbi.2010.01.014
Scopus ID 77951298112
Erfassungsdatum 2010-12-31
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