Abstract:
:Lon is an ATPase associated with cellular activities (AAA+) protease that controls cell division in response to stress and also degrades misfolded and damaged proteins. Subunits of Lon are known to assemble into ring-shaped homohexamers that enclose an internal degradation chamber. Here, we demonstrate that hexamers of Escherichia coli Lon also interact to form a dodecamer at physiological protein concentrations. Electron microscopy of this dodecamer reveals a prolate structure with the protease chambers at the distal ends and a matrix of N domains forming an equatorial hexamer-hexamer interface, with portals of ∼45 Å providing access to the enzyme lumen. Compared with hexamers, Lon dodecamers are much less active in degrading large substrates but equally active in degrading small substrates. Our results support a unique gating mechanism that allows the repertoire of Lon substrates to be tuned by its assembly state.
journal_name
Proc Natl Acad Sci U S Aauthors
Vieux EF,Wohlever ML,Chen JZ,Sauer RT,Baker TAdoi
10.1073/pnas.1307066110subject
Has Abstractpub_date
2013-05-28 00:00:00pages
E2002-8issue
22eissn
0027-8424issn
1091-6490pii
1307066110journal_volume
110pub_type
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