Two Different Oligomeric States of the RuvB Branch Migration Motor Protein as Revealed by Electron Microscopy

doi:10.1006/jsbi.2000.4290

Journal of Structural Biology

Volume 131, Issue 2, August 2000, Pages 83-89

https://doi.org/10.1006/jsbi.2000.4290 Get rights and content

Abstract

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.

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This article has been retracted: please see Elsevier Policy on Article Withdrawal (http://www.elsevier.com/locate/withdrawalpolicy).
This article has been retracted at the request of the authors.
It was brought to our attention that Figure 3B of this paper, which shows very efficient labeling of the RuvB oligomer, contains an image that was possibly fabricated. An allegation of scientific misconduct was therefore lodged through the appropriate channel at Brandeis University against the paper’s first author, Kelsey Anthony. Pursuant to the university’s Research Misconduct Policy, the relevant facts and materials were collected by the Senior Research Officer, and this material was presented to the Provost. This investigation concluded that Kelsey Anthony did carry out scientific misconduct and that none of the paper’s co-authors were privy to her actions. In addition, an external independent review was obtained by Brandeis University that concurred with these findings. The external review also substantiated that the EM images and data in Figures 4C and 4D, which show the labeling of the 50S, were not falsified.
The fabrication of RuvB labeling gave the impression of very efficient labeling, but this is not the case. While the gold labeling of 50S was successful, the misconduct of the first author noted above leaves us no other option but to retract this publication. We apologize to our colleagues for any loss of time or resources caused by this publication.
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Regular ArticleTwo Different Oligomeric States of the RuvB Branch Migration Motor Protein as Revealed by Electron Microscopy

Abstract

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

J. Struct. Biol.

J. Mol. Biol.

Curr. Biol.

Curr. Opin. Struct. Biol.

J. Struct. Biol.

J. Mol. Biol.

Trends Biochem. Sci.

Structure

J. Struct. Biol.

J. Mol. Biol.

J. Mol. Biol.

Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria

Nature

Regular Article
Two Different Oligomeric States of the RuvB Branch Migration Motor Protein as Revealed by Electron Microscopy