Journal list menu

Volume 314, Issue 1 p. 10-12
Full-length article
Free Access

Structure of UvrABC excinuclease—UV-damaged DNA complexes studied by flow linear dichroism DNA curved by UvrB and UvrC

Masayuki Takahashi

Corresponding Author

Masayuki Takahashi

Groupe de Cancérogénèse et de Mutagénèse Moléculaire et Structurale, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15 rue René Descartes, F-67084 Strasbourg Cedex, France

Correspondence address: M. Takahashi, Groupe de Cancérogénèse et de Mutagénèse Moléculaire et Structurale, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15 rue René Descartes, F-67084 Strasbourg Cedex, FranceSearch for more papers by this author
Elisabeth Bertrand-Burggraf

Elisabeth Bertrand-Burggraf

Groupe de Cancérogénèse et de Mutagénèse Moléculaire et Structurale, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15 rue René Descartes, F-67084 Strasbourg Cedex, France

Search for more papers by this author
Robert P.P. Fuchs

Robert P.P. Fuchs

Groupe de Cancérogénèse et de Mutagénèse Moléculaire et Structurale, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15 rue René Descartes, F-67084 Strasbourg Cedex, France

Search for more papers by this author
Bengt Nordén

Bengt Nordén

Department of Physical Chemistry, Chalmers University of Technology, S-41296 Gothenburg, Sweden

Search for more papers by this author
First published: December 07, 1992
Citations: 8

Abstract

The interaction between UvrABC excinuclease from Escherichia coli and ultraviolet light-(UV) damaged DNA was studied by flow linear dichroism. The dichroism signal from DNA was drastically decreased in intensity upon incubation with UvrA and UvrB or whole enzyme in the presence off effector ATP. The change was specific for UV-damaged DNA, and a concluded suppressed DNA orientation suggests the wrapping of DNA around the protein. The incubation with the UvrC subunit alone also somewhat reduces the signal, however, in this case the change was smaller and not specific for UV-damaged DNA. The structural modification of DNA, promoted by the (UvrA2-UvrB) complex probably facilitates or stabilizes the interaction of the UvrC subunit with DNA for the excision.