Journal of Biological Chemistry
Volume 274, Issue 32, 6 August 1999, Pages 22437-22444
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ENZYMOLOGY
TIP49b, a New RuvB-like DNA Helicase, Is Included in a Complex Together with Another RuvB-like DNA Helicase, TIP49a*

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We previously reported that TIP49a is a novel mammalian DNA helicase showing structural similarity with the bacterial recombination factor RuvB. In this study, we isolated a newTIP49a-related gene, termed TIP49b, from human and yeast cells. TIP49b also resembled RuvB, thus suggesting that TIP49a and TIP49b are included in a gene family. Like TIP49a, TIP49b was abundantly expressed in the testis and thymus. Enzyme assays revealed that TIP49b was an single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase. Most of the enzymatic properties of TIP49b were the same as those of TIP49a, whereas the polarity of TIP49b DNA helicase activity (5′ to 3′) was the opposite to that of TIP49a. TIP49b and TIP49a bound to each other and were included in the same complex of ∼700 kDa in a cell. We found thatTIP49b was an essential gene for the growth ofSaccharomyces cerevisiae, as is the TIP49agene, suggesting that TIP49b does not complement the TIP49a function and vice versa. From these observations, we suggest that TIP49b plays an essential role in the cellular processes involved in DNA metabolism.

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*

This work supported in part by a grant-in-aid for Scientific Research of The Japanese Ministry of Education, Science, Sports, and Culture.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide and amino acid sequences reported in this paper have been submitted to the DDBJ/GenBankTM/EBI data banks with accession number AB024301

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A research fellow of The Japan Society For The Promotion Of Science.