Two different oligomeric states of the RuvB branch migration motor protein as revealed by electron microscopy

Tomoko Miyata, Kazuhiro Yamada, Hiroshi Iwasaki, Hideo Shinagawa, Kosuke Morikawa, Kouta Mayanagi

研究成果: Contribution to journalArticle査読

46 被引用数 (Scopus)

抄録

In prokaryotes, the RuvA, B, and C proteins play major roles at the late stage of DNA homologous recombination, where RuvB complexed with RuvA acts as an ATP-dependent motor for branch migration. The oligomeric structures of negatively stained and frozen hydrated RuvB from Thermus thermophilus HB8 were investigated by electron microscopy. RuvB oligomers free of DNA formed a ring structure of about 14 nm in diameter. The averaged top view image clearly indicated a sevenfold symmetry, suggesting that it exists as a heptamer. The RuvB oligomers complexed with duplex DNA formed a smaller ring of about 13 nm in diameter. The averaged top view images represented a sixfold symmetry. This difference in oligomerization indicates that the oligomeric structure of RuvB may convert from a heptamer to a hexamer upon DNA binding. In addition, this finding provides the lesson that great care should be taken in investigating the subunit organizations of DNA binding proteins, because their oligomeric states are more sensitive to DNA interactions than expected. (C) 2000 Academic Press.

本文言語英語
ページ(範囲)83-89
ページ数7
ジャーナルJournal of structural biology
131
2
DOI
出版ステータス出版済み - 2000
外部発表はい

All Science Journal Classification (ASJC) codes

  • 構造生物学

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