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

J. Biol. Chem., Vol. 282, Issue 39, 28474-28484, September 28, 2007

This Article Full Text Full Text (PDF) All Versions of this Article: 282/39/28474    most recent M704672200v1 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 Das, S. Articles by Hazra, T. K. Search for Related Content PubMed PubMed Citation Articles by Das, S. Articles by Hazra, T. K. Social Bookmarking                      What's this?

Stimulation of NEIL2-mediated Oxidized Base Excision Repair via YB-1 Interaction during Oxidative Stress^*

Soumita Das, Ranajoy Chattopadhyay, Kishor K. Bhakat, Istvan Boldogh, Kimitoshi Kohno^¶, Rajendra Prasad^||, Samuel H. Wilson^||, and Tapas K. Hazra¹

From the Sealy Center for Molecular Medicine and Departments of Biochemistry and Molecular Biology and Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas 77555, the ^¶Department of Molecular Biology, University of Occupational and Environmental Health School of Medicine, Iseigaoka, Kitakyushu, Japan, and the ^||Laboratory of Structural Biology, NIEHS, National Institutes of Health, Research Triangle Park, North Carolina 27709

The recently characterized enzyme NEIL2 (Nei-like-2), one of the four oxidized base-specific DNA glycosylases (OGG1, NTH1, NEIL1, and NEIL2) in mammalian cells, has poor base excision activity from duplex DNA. To test the possibility that one or more proteins modulate its activity in vivo, we performed mass spectrometric analysis of the NEIL2 immunocomplex and identified Y box-binding (YB-1) protein as a stably interacting partner of NEIL2. We show here that YB-1 not only interacts physically with NEIL2, but it also cooperates functionally by stimulating its base excision activity by 7-fold. Moreover, YB-1 interacts with the other NEIL2-associated BER proteins, namely, DNA ligase III and DNA polymerase and thus could form a large multiprotein complex. YB-1, normally present in the cytoplasm, translocates to the nucleus during UVA-induced oxidative stress, concomitant with its increased association with and activation of NEIL2. NEIL2-initiated base excision activity is significantly reduced in YB-1-depleted cells. YB-1 thus appears to have a novel regulatory role in NEIL2-mediated repair under oxidative stress.

Received for publication, June 6, 2007 , and in revised form, August 7, 2007.

^* This work was supported in part by United States Public Health Service Grants CA102271 (to T. K. H.), P01 AG021830 (to I. B. and T. K. H.), P01 ES06676 (to T. K. H.), CA81063 (to R. C.), and E508457 (to K. K. B.), and the Intramural Research Program of the National Institutes of Health, NIEHS. 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.

¹ To whom correspondence should be addressed: 6.136 Medical Research Bldg., Route 1079; Galveston, TX 77555. Tel.: 409-772-6308; Fax: 409-747-8608; E-mail: tkhazra{at}utmb.edu.

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

This article has been cited by other articles:

				M. L. Hegde, C. A. Theriot, A. Das, P. M. Hegde, Z. Guo, R. K. Gary, T. K. Hazra, B. Shen, and S. Mitra Physical and Functional Interaction between Human Oxidized Base-specific DNA Glycosylase NEIL1 and Flap Endonuclease 1 J. Biol. Chem., October 3, 2008; 283(40): 27028 - 27037. [Abstract] [Full Text] [PDF]