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The La antigen associates with the human telomerase ribonucleoprotein and influences telomere length in vivo

Published online by Cambridge University Press:  27 July 2001

LANCE P. FORD
Affiliation:
The University of Texas Southwestern Medical Center, The Department of Cell Biology, Dallas, Texas 75390-9039, USA
JERRY W. SHAY
Affiliation:
The University of Texas Southwestern Medical Center, The Department of Cell Biology, Dallas, Texas 75390-9039, USA
WOODRING E. WRIGHT
Affiliation:
The University of Texas Southwestern Medical Center, The Department of Cell Biology, Dallas, Texas 75390-9039, USA
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Abstract

La is an important component of ribonucleoprotein complexes and telomerase is a ribonucleoprotein that compensates for the shortening of the ends of linear DNA by adding telomeric repeats onto the ends of chromosomes by using an integral RNA as the template. We have identified a direct and specific interaction between La and the RNA component of human telomerase. Antibodies specific to La precipitate the human telomerase ribonucleoprotein complex derived from tumor cells, telomerase immortalized normal cells, and in vitro transformed cells. Overexpression of La in both experimentally immortalized human cells and prostate cancer cells results in gradual telomere shortening. Our results demonstrate that La can associate with telomerase and its expression level can influence telomere homeostasis in vivo.

Type
REPORTS
Copyright
© 2001 RNA Society

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