HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 279, Issue 20, 20692-20698, May 14, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/20/20692    most recent M400231200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kikuma, T. Articles by Murakami, Y. Search for Related Content PubMed PubMed Citation Articles by Kikuma, T. Articles by Murakami, Y. Social Bookmarking                      What's this?

Dbp9p, a Member of the DEAD Box Protein Family, Exhibits DNA Helicase Activity^*

Takashi Kikuma, Masaya Ohtsu, Takahiko Utsugi, Shoko Koga, Kohji Okuhara, Toshihiko Eki, Fumihiro Fujimori, and Yasufumi Murakami

From the Department of Biological Science and Technology, Faculty of Industrial Science and Technology, Tokyo University of Science, Noda, Chiba 278-8510, Japan and the Department of Ecological Engineering, Toyohashi University of Technology, Toyohashi, Aichi 441-8580, Japan

The yeast Dbp9p is a member of the DEAD box family of RNA helicases, which are thought to be involved in RNA metabolism. Dbp9p seems to function in ribosomal RNA biogenesis, but it has not been biochemically characterized. To analyze the enzymatic characteristics of the protein, we expressed a recombinant Dbp9p in Escherichia coli and purified it to homogeneity. The purified protein exhibited RNA unwinding and binding activity in the absence of NTP, and this activity was abolished by a mutation in the RNA-binding domain. We then characterized the ATPase activity of Dbp9p with respect to cofactor specificity; the activity was found to be severely inhibited by yeast total RNA and moderately inhibited by poly(U), poly(A), and poly(C) but to be stimulated by yeast genomic DNA and salmon sperm DNA. In addition, Dbp9p exhibited DNA-DNA and DNA-RNA helicase activity in the presence of ATP. These results indicate that Dbp9p has biochemical characteristics unique among DEAD box proteins.

Received for publication, January 9, 2004 , and in revised form, March 1, 2004.

^* This work was supported by grants-in-aid from the New Energy Developments Organization (NEDO), the Organization for Pharmaceutical Safety and Research, and the Ministry of Education, Culture, Sports, Science, and Technology of Japan. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Biological Science and Technology, Faculty of Industrial Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda-shi, Chiba 278-8510, Japan. Tel.: 81-4-7124-1501 (ext. 4408); Fax: 81-4-7122-1360; E-mail: yasufumi{at}rs.noda.tus.ac.jp.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				H. H. Liu, J. Liu, S. L. Fan, M. Z. Song, X. L. Han, F. Liu, and F. F. Shen Molecular cloning and characterization of a salinity stress-induced gene encoding DEAD-box helicase from the halophyte Apocynum venetum J. Exp. Bot., February 13, 2008; (2008) erm355v1. [Abstract] [Full Text] [PDF]

				P. Linder Dead-box proteins: a family affair--active and passive players in RNP-remodeling Nucleic Acids Res., September 10, 2006; 34(15): 4168 - 4180. [Abstract] [Full Text] [PDF]

				S. Granneman, C. Lin, E. A. Champion, M. R. Nandineni, C. Zorca, and S. J. Baserga The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis Nucleic Acids Res., June 13, 2006; 34(10): 3189 - 3199. [Abstract] [Full Text] [PDF]

				K. A. Bernstein, S. Granneman, A. V. Lee, S. Manickam, and S. J. Baserga Comprehensive Mutational Analysis of Yeast DEXD/H Box RNA Helicases Involved in Large Ribosomal Subunit Biogenesis Mol. Cell. Biol., February 15, 2006; 26(4): 1195 - 1208. [Abstract] [Full Text] [PDF]

				H. Uhlmann-Schiffler, C. Jalal, and H. Stahl Ddx42p--a human DEAD box protein with RNA chaperone activities Nucleic Acids Res., January 5, 2006; 34(1): 10 - 22. [Abstract] [Full Text] [PDF]

				F. Estruch, C. A. Hodge, S. Rodriguez-Navarro, and C. N. Cole Physical and Genetic Interactions Link the Yeast Protein Zds1p with mRNA Nuclear Export J. Biol. Chem., March 11, 2005; 280(10): 9691 - 9697. [Abstract] [Full Text] [PDF]

				S. Rocak, B. Emery, N. K. Tanner, and P. Linder Characterization of the ATPase and unwinding activities of the yeast DEAD-box protein Has1p and the analysis of the roles of the conserved motifs Nucleic Acids Res., February 17, 2005; 33(3): 999 - 1009. [Abstract] [Full Text] [PDF]