spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

First published online 30 June 2009
doi: 10.1242/jcs.048066

Journal of Cell Science 122, 2613-2622 (2009)
Published by The Company of Biologists 2009
This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary Material
Right arrow All Versions of this Article:
jcs.048066v1
122/15/2613    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Related articles in JCS
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Google Scholar
Right arrow Articles by Oh, W.
Right arrow Articles by Song, J.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Oh, W.
Right arrow Articles by Song, J.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Research Article

PML-IV functions as a negative regulator of telomerase by interacting with TERT

Wonkyung Oh1,*, Jaewang Ghim1,*,{ddagger}, Eun-Woo Lee1, Mi-Ran Yang1, Eui Tae Kim2, Jin-Hyun Ahn2 and Jaewhan Song1,§

1 Department of Biotechnology and Bioengineering, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon, Korea
2 Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon, Korea

§ Author for correspondence (e-mail: jso678{at}skku.edu)

Accepted 15 April 2009

Maintaining proper telomere length requires the presence of the telomerase enzyme. Here we show that telomerase reverse transcriptase (TERT), a catalytic component of telomerase, is recruited to promyelocytic leukemia (PML) nuclear bodies through its interaction with PML-IV. Treatment of interferon-{alpha} (IFN{alpha}) in H1299 cells resulted in the increase of PML proteins with a concurrent decrease of telomerase activity, as previously reported. PML depletion, however, stimulated telomerase activity that had been inhibited by IFN{alpha} with no changes in TERT mRNA levels. Upon treatment with IFN{alpha}, exogenous TERT localized to PML nuclear bodies and binding between TERT and PML increased. Immunoprecipitation and immunofluorescence analyses showed that TERT specifically bound to PML-IV. Residues 553-633 of the C-terminal region of PML-IV were required for its interaction with the TERT region spanning residues 1-350 and 595-946. The expression of PML-IV and its deletion mutant, 553-633, suppressed intrinsic telomerase activity in H1299. TERT-mediated immunoprecipitation of PML or the 553-633 fragment demonstrated that these interactions inhibited telomerase activity. H1299 cell lines stably expressing PML-IV displayed decreased telomerase activity with no change of TERT mRNA levels. Accordingly, telomere length of PML-IV stable cell lines was shortened. These results indicate that PML-IV is a negative regulator of telomerase in the post-translational state.

Key words: Telomerase, TERT, PML, TERC, PML nuclear bodies


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

Related articles in JCS:

PML-IV puts the brakes on telomerase

JCS 2009 122: 1502. [Full Text]  





© The Company of Biologists Ltd 2009