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Published online before print February 20, 2004, 10.1101/gad.1171804
GENES & DEVELOPMENT 18:387-396, 2004
©2004 by Cold Spring Harbor Laboratory Press; ISSN 0890-9369/ $5.00
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RESEARCH PAPER

Nucleolar protein PinX1p regulates telomerase by sequestering its protein catalytic subunit in an inactive complex lacking telomerase RNA

Jue Lin and Elizabeth H. Blackburn1

Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, California 94143-2200, USA

Human TRF1-binding protein PinX1 inhibits telomerase activity. Here we report that overexpression of yeast PinX1p (yPinX1p) results in shortened telomeres and decreased in vitro telomerase activity. yPinX1p coimmunoprecipitated withyeast telomerase protein Est2p even in cells lacking the telomerase RNA TLC1, or the telomerase-associated proteins Est1p and Est3p. Est2p regions required for binding to yPinX1p or TLC1 were similar. Furthermore, we found two distinct Est2p complexes exist, containing either yPinX1p or TLC1. Levels of Est2p–yPinX1p complex increased when TLC1 was deleted and decreased when TLC1 was overexpressed. Hence, we propose that yPinX1p regulates telomerase by sequestering its protein catalytic subunit in an inactive complex lacking telomerase RNA.

[Keywords: Telomerase regulation; telomerase sequestration; alternative telomerase complex; PinX1–telomerase protein complex]

Received November 24, 2003; revised version accepted December 30, 2003.

Article published online ahead of print. Article and publication date are at http://www.genesdev.org/cgi/doi/10.1101/gad.1171804.

Supplemental material is available at http://www.genesdev.org.

1 Corresponding author.

E-MAIL telomer{at}itsa.ucsf.edu; FAX (415) 514-2913.


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