TY - JOUR
T1 - Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits
AU - Stahlberg, Henning
AU - Kutejová, Eva
AU - Suda, Kitaru
AU - Wolpensinger, Bettina
AU - Lustig, Ariel
AU - Schatz, Gottfried
AU - Engel, Andreas
AU - Suzuki, Carolyn K.
PY - 1999/6/8
Y1 - 1999/6/8
N2 - 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.
AB - 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.
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U2 - 10.1073/pnas.96.12.6787
DO - 10.1073/pnas.96.12.6787
M3 - Article
C2 - 10359790
AN - SCOPUS:0033536010
SN - 0027-8424
VL - 96
SP - 6787
EP - 6790
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 12
ER -