Identification of a novel helicase activity unwinding branched DNAs from the hyperthermophilic archaeon, Pyrococcus furiosus

doi:10.1074/jbc.M413417200

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Papers In Press, published online ahead of print January 27, 2005
J. Biol. Chem, 10.1074/jbc.M413417200
Submitted on November 29, 2004
Revised on January 11, 2005
Accepted on January 27, 2005

Identification of a novel helicase activity unwinding branched DNAs from the hyperthermophilic archaeon, Pyrococcus furiosus

Ryosuke Fujikane, Kayoko Komori, Hideo Shinagawa, and Yoshizumi Ishino

Department of Genetic ResourcesTechnology, Kyushu University, Fukuoka, Fukuoka 812-8581

Corresponding Author: ishino{at}agr.kyushu-u.ac.jp

To identify the branch migration activity in archaea, we fractionated P. furiosus cell extracts by several chromatographies and assayed for ATP-dependent resolution of synthetic Holliday junctions. The target activity was identified in the column fractions, and the optimal reaction conditions for the branch migration activity were determined using the partially purified fraction. We successfully cloned the corresponding gene by screening a heat-stable protein library made by P. furiosus genomic DNA. The gene, hjm (Holliday junction migration), encodes a protein composed of 720 amino acids. The Hjm protein is conserved in Archaea and belongs to the helicase superfamily 2. A homology search revealed that Hjm shares sequence similarity with the human PolQ, HEL308, and Drosophila Mus308 proteins, which are involved in a DNA repair, whereas no similar sequences were found in bacteria and yeast. The Hjm helicase may play a central role in the repair systems of organisms living in extreme environments.

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