Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits.

Abstract:

:Lon (or La) is a soluble, homooligomeric ATP-dependent protease. Mass determination and cryoelectron microscopy of pure mitochondrial Lon from Saccharomyces cerevisiae identify Lon as a flexible ring-shaped heptamer. In the presence of ATP or 5'-adenylylimidodiphosphate, most of the rings are symmetric and resemble other ATP-driven machines that mediate folding and degradation of proteins. In the absence of nucleotides, most of the rings are distorted, with two adjacent subunits forming leg-like protrusions. These results suggest that asymmetric conformational changes serve to power processive unfolding and translocation of substrates to the active site of the Lon protease.

authors

Stahlberg H,Kutejová E,Suda K,Wolpensinger B,Lustig A,Schatz G,Engel A,Suzuki CK

doi

10.1073/pnas.96.12.6787

keywords:

subject

Has Abstract

pub_date

1999-06-08 00:00:00

pages

6787-90

issue

12

eissn

0027-8424

issn

1091-6490

journal_volume

96

pub_type

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