| Literature DB >> 17502110 |
Etsuko Tanaka1, Hirokazu Fukuda, Katsuhiko Nakashima, Naoto Tsuchiya, Hiroyuki Seimiya, Hitoshi Nakagama.
Abstract
The biological function of hnRNP family proteins is widely diverse and involved in pre-mRNA processing, transcriptional regulation, recombination, and telomere maintenance. In the course of our study on the elucidation of biological functions of minisatellite DNA, we isolated several nuclear proteins that bind to the mouse minisatellite Pc-1, which consists of a tandem array of d(GGCAG) repeats, from NIH3T3 cells. One of the minisatellite binding proteins, MNBP-A, which binds to a single-stranded G-rich strand of the Pc-1 repeat, was proven identical to the hnRNP A3. Recombinant hnRNP A3 was demonstrated to bind to the single-stranded telomeric d(TTAGGG) repeat with much higher affinity than the d(GGCAG) repeat. Binding of hnRNP A3 to the single-stranded telomeric repeat protected the repeat from nuclease attack, and inhibited both telomerase reaction and DNA synthesis in vitro. These results suggest a possible biological role of hnRNP A3 in the stable maintenance of telomere repeats.Entities:
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Year: 2007 PMID： 17502110 DOI： 10.1016/j.bbrc.2007.04.177
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575