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M111068200v1
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Papers In Press, published online ahead of print December 18, 2001
J. Biol. Chem, 10.1074/jbc.M111068200
Submitted on November 19, 2001
Revised on December 17, 2001
Accepted on December 17, 2001

Two independent regions of human telomerase reverse transcriptase (hTERT) are important for its oligomerization and telomerase activity

Kuniaki Arai, Kenkichi Masutomi, Shilagardy Khurts, Shuichi Kaneko, Kenichi Kobayashi, and Seishi Murakami

Dept. Molecular Oncogoly, Cancer Research Institute,Kanazawa University, Kanazawa, Ishikawa 920-0934

Corresponding Author: semuraka{at}kenroku.kanazawa-u.ac.jp

Human telomerase reverse transcriptase (hTERT), the catalytic subunit of telomerase, contains motifs conserved among reverse transcriptases. Several nucleic acid-dependent polymerases (NdNPs) that share a “fingers, palm and thumb substructure” were shown to oligomerize. Here we demonstrate that hTERT also has this ability using partially purified recombinant hTERTs and mammalian cells coexpressing differently tagged hTERTs. Human-TR, by contrast, has no effect on the structural oligomerization of hTERTs. Therefore, hTERT has an intrinsic ability of oligomerization in the absence of hTR. We identified two separate regions as essential for the oligomerization. The regions, aa 301-538 (amino-terminal region) and aa 914-928 (carboxy-terminal region), are outside the fingers and palm substructure covering motif T to D, and interact with each other in vivo. A substituted mutant of hTERT, hTERT-D712A-V713I which was reported as dominant negative form of hTERT, bound to the wild-type hTERT and inhibited its telomerase activity transiently expressed in telomerase-negative finite normal human fibroblast. The truncated forms of hTERT containing the binding region to the wild-type hTERT partially inhibited the telomerase activity, probably by preventing the wild-type hTERT from forming an oligomer. Taken together, the oligomerization of hTERT is an important step for telomerase activity.


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