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Telomere- and telomerase-interacting protein that unfolds telomere G-quadruplex and promotes telomere extension in mammalian cells.

Authors: Wang, F  Tang, ML  Zeng, ZX  Wu, RY  Xue, Y  Hao, YH  Pang, DW  Zhao, Y  Tan, Z 
Citation: Wang F, etal., Proc Natl Acad Sci U S A. 2012 Dec 11;109(50):20413-8. doi: 10.1073/pnas.1200232109. Epub 2012 Nov 26.
Pubmed: (View Article at PubMed) PMID:23184978
DOI: Full-text: DOI:10.1073/pnas.1200232109

Telomere extension by telomerase is essential for chromosome stability and cell vitality. Here, we report the identification of a splice variant of mammalian heterogeneous nuclear ribonucleoprotein A2 (hnRNP A2), hnRNP A2*, which binds telomeric DNA and telomerase in vitro. hnRNP A2* colocalizes with telomerase in Cajal bodies and at telomeres. In vitro assays show that hnRNP A2* actively unfolds telomeric G-quadruplex DNA, exposes 5 nt of the 3' telomere tail and substantially enhances the catalytic activity and processivity of telomerase. The expression level of hnRNP A2* in tissues positively correlates with telomerase activity, and overexpression of hnRNP A2* leads to telomere elongation in vivo. Thus, hnRNP A2* plays a positive role in unfolding telomere G-quadruplexes and in enhancing telomere extension by telomerase.

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CRRD Object Information
CRRD ID: 11567256
Created: 2016-12-03
Species: All species
Last Modified: 2016-12-03
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.