CU Molecular, Cellular, and Developmental Biology
MCDB Home > faculty > FacultyPublications > CechTRPublications > Telomerase RNA bound by protein motifs s ... elomerase reverse transcriptase
Document Actions

Telomerase RNA bound by protein motifs s ... elomerase reverse transcriptase


Telomerase RNA bound by protein motifs specific to telomerase reverse transcriptase.

68

Telomerase reverse transcriptase (TERT) differs from many other reverse transcriptases in that it remains stably associated with its template-containing RNA subunit. Elements of TERT involved in binding the RNA subunit have now been identified by mutagenesis and in vitro reconstitution of the Tetrahymena ribonucleoprotein complex. Mutations in the reverse transcriptase motifs of TERT reduced activity as expected but did not greatly reduce its binding to the telomerase RNA. In contrast, all mutations in the T and CP motifs dramatically reduced RNA binding. We therefore suggest that the T and CP motifs of TERT function to hold on to the telomerase RNA, leaving the RNA template region free to translocate through the RT domain.


Bryan TM, Goodrich KJ, Cech TR

Molecular cell

2000-08-01 00:00

6

2

493-9

Amino Acid Sequence,Binding Sites,Consensus Sequence,Conserved Sequence,Molecular Sequence Data,Mutagenesis, Site-Directed,Point Mutation,RNA,RNA-Directed DNA Polymerase,Recombinant Proteins,Telomerase,Thermus thermophilus,Recombinant Proteins,RNA,RNA-Directed DNA Polymerase,Telomerase

Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309, USA

Mol. Cell


1097-2765


S1097-2765(00)00048-4


280

True

10983995

Thomas Cech
University of Colorado Contact Us  |   Legal & Trademarks  |  Privacy