Premium
Human telomerase contains two cooperating telomerase RNA molecules
Author(s) -
Wenz Christian,
Enenkel Barbara,
Amacker Mario,
Kelleher Colleen,
Damm Klaus,
Lingner Joachim
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.13.3526
Subject(s) - telomerase , biology , telomerase rna component , telomere , rna , telomerase reverse transcriptase , reverse transcriptase , microbiology and biotechnology , protein subunit , transcription (linguistics) , biochemistry , dna , gene , linguistics , philosophy
Telomerase uses a short stretch of its intrinsic RNA molecule as template for telomere repeat synthesis. Reverse transcription of the RNA template is catalyzed by the telomerase reverse transcriptase (TERT) protein subunit. We demonstrate that human telomerase reconstituted from recombinant TERT and telomerase RNA runs as a dimer on a gel filtration column and that it contains two telomerase RNA molecules. Significantly, a telomerase heterodimer reconstituted from wild‐type and mutant telomerase RNA is barely active when compared with the wild‐type homodimer. We conclude that the telomerase RNA templates in the active enzyme are interdependent and functionally cooperate with each other. We discuss models that may explain the biological and enzymatic roles of telomerase dimerization.