REVIEW: Polypeptide Components of Telomere Nucleoprotein Complex
A. N. Kuimov
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State
University, Moscow 119899, Russia; fax: (7-095) 939-3181; E-mail:
kuimov@genebee.msu.su
Received July 25, 2003; Revision received September 8, 2003
Chromosome telomeres of humans and many model organisms contain a
structure called a t-loop, which is maintained by TERF, TINF2, Pot1,
and other proteins. Increase in TERF1 concentration prevents telomere
elongation by telomerase. Decrease in TERF2 concentration (preventing
t-loop formation) is accompanied by blockade of proliferation and
appearance of other signs of cellular senescence in experiments.
Natural regulation of TERF1 involves tankyrase, ATM protein kinase, and
fluctuations of the protein level across a cell cycle. The telomere
nucleoprotein complex also interacts with various polypeptide
macromolecules (e.g., Sir2, PinX1, Rap1, Ku, Rad50/Mre11/Nbs1)
responsible for heterochromatin formation, modulation of telomerase
activity, DNA repair, and signaling to other cell compartments about
telomere state. Study of structure and functioning of telomere
nucleoprotein complex may contribute to elucidation of poorly
understood mechanisms of aging and processes of tumor transformation of
cells.
KEY WORDS: telomeres, telomerase, TERF, tankyrase, Ku,
Rad50/Mre11/Nbs1, replicative senescence, immortalization