Distinct quaternary structures of the AAA+ Lon protease control substrate degradation.

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.

authors

Vieux EF,Wohlever ML,Chen JZ,Sauer RT,Baker TA

doi

10.1073/pnas.1307066110

subject

Has Abstract

pub_date

2013-05-28 00:00:00

pages

E2002-8

issue

22

eissn

0027-8424

issn

1091-6490

pii

1307066110

journal_volume

110

pub_type

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