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

J. Biol. Chem., Vol. 279, Issue 21, 22362-22370, May 21, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/21/22362    most recent M313647200v1 Alert me when this article is cited 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 Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Békési, A. Articles by Vértessy, B. G. Search for Related Content PubMed PubMed Citation Articles by Békési, A. Articles by Vértessy, B. G. Social Bookmarking                      What's this?

Developmental Regulation of dUTPase in Drosophila melanogaster^*

Angéla Békési, Imre Zagyva, Éva Hunyadi-Gulyás, Veronika Pongrácz, Júlia Kovári, Ágnes O. Nagy, Anna Erdei¶, Katalin F. Medzihradszky||, and Beáta G. Vértessy**

From the Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, H-1518 Budapest, Hungary, the Mass Spectrometry Facility, Biological Research Center, Hungarian Academy of Sciences, H-6701 Szeged, Hungary, the ^¶Department of Immunology, Eötvös Loránd University of Science, H-1518 Budapest, Hungary, and the ^||Department of Pharmaceutical Chemistry, School of Pharmacy, University of California San Francisco, San Francisco, California 94143-0446

dUTPase prevents uracil incorporation into DNA by strict regulation of the cellular dUTP:dTTP ratio. Lack of the enzyme initiates thymineless cell death, prompting studies on enzyme regulation. We investigated expression pattern and localization of Drosophila dUTPase. Similarly to human, two isoforms of the fly enzyme were identified at both mRNA and protein levels. During larval stages, a drastic decrease of dUTPase expression was demonstrated at the protein level. In contrast, dUTPase mRNAs display constitutive character throughout development. A putative nuclear localization signal was identified in one of the two isoforms. However, immunohistochemistry of ovaries and embryos did not show a clear correlation between the presence of this signal and subcellular localization of the protein, suggesting that the latter may be perturbed by additional factors. Results are in agreement with a multilevel regulation of dUTPase in the Drosophila proteome, possibly involving several interacting protein partners of the enzyme. Using independent approaches, the existence of such macromolecular partners was verified.

Received for publication, December 12, 2003 , and in revised form, February 27, 2004.

^* This work was supported by Grants T 034120, TS 044730, and M 27852 (to B. G. V.) and Grant T 037916 (to K. F. M.) from the Hungarian National Research Foundation; Grant 55000342 (to B. G. V.) from the Howard Hughes Medical Institutes; and a grant from the Alexander von Humboldt Foundation, Germany (to B. G. V.). 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: Institute of Enzymology, BRC, Hungarian Academy of Sciences, P. O. Box 7, H-1518 Budapest, Hungary. Tel.: 361-279-3100; Fax: 361-466-5465; E-mail: vertessy{at}enzim.hu.

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

This article has been cited by other articles:

				J. Toth, B. Varga, M. Kovacs, A. Malnasi-Csizmadia, and B. G. Vertessy Kinetic Mechanism of Human dUTPase, an Essential Nucleotide Pyrophosphatase Enzyme J. Biol. Chem., November 16, 2007; 282(46): 33572 - 33582. [Abstract] [Full Text] [PDF]