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J. Biol. Chem., Vol. 282, Issue 39, 28474-28484, September 28, 2007
Stimulation of NEIL2-mediated Oxidized Base Excision Repair via YB-1 Interaction during Oxidative Stress*![]() ![]() ![]() ![]() 1
From the
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
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.
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