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Journal of Biochemistry Advance Access published online on December 6, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn166
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© The authors 2008. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Characterization of Moloney Murine Leukaemia Virus/Avian Myeloblastosis Virus Chimeric Reverse Transcriptases

Kiyoshi Yasukawa*, Masaki Mizuno and Kuniyo Inouye

Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502

*To whom correspondence should be addressed. Dr. Kiyoshi Yasukawa Tel: +81-75-753-6267, Fax: +81-75-753-6265, E-mail: yasukawa{at}kais.kyoto-u.ac.jp

Received November 19, 2008; Accepted December 1, 2008


  Abstract

Reverse transcriptases (RTs) from Moloney murine leukaemia virus (MMLV) and avian myeloblastosis virus (AMV) contain all the fingers, palm, thumb, connection, and RNase H domains. The fingers, palm, and thumb domains are thought to be involved in the reverse transcription activity, and the RNase H domain is in the RNase H activity. In this study, we characterized four chimeric RTs which comprise one of the fingers, palm, thumb, and RNase H domains originated from AMV RT and the other three and connection domains originated from MMLV RT. Unexpectedly, all chimeric RTs exhibited the same characteristics: their specific reverse transcription activities decreased to less than 0.1% of that of MMLV RT, while their specific RNase H activities were approximately 20% of that of MMLV RT. The decreases in the two activities of the chimeric RTs were ascribed to the decreases in kcat. Based on that the reverse transcription activity of MMLV RT was impaired by substituting its RNase H domain with that from AMV RT, we propose that in MMLV RT, there might be an interaction between the fingers/palm/thumb domain and the RNase H domain.

Key Words: avian myeloblastosis virus, chimeric enzyme, Moloney murine leukaemia virus, reverse transcriptase, RNase H


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