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

Henning Stahlberg, Eva Kutejová, Kitaru Suda, Bettina Wolpensinger, Ariel Lustig, Gottfried Schatz, Andreas Engel, Carolyn K. Suzuki

Research output: Contribution to journalArticlepeer-review

104 Scopus citations

Abstract

Lon (or La) is a soluble, homooligomerie 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.

Original languageEnglish (US)
Pages (from-to)6787-6790
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number12
DOIs
StatePublished - Jun 8 1999

All Science Journal Classification (ASJC) codes

  • General

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