Oligomerization of the telomerase reverse transcriptase from Euplotes crassus.

ABSTRACT: The telomerase ribonucleoprotein reverse transcriptase uses its RNA subunit as a template to synthesize telomeric repeats and maintain telomere tracts on chromosome ends. In the ciliate Euplotes crassus, the core telomerase ribonucleoprotein particle undergoes a developmentally programmed assembly into three higher order complexes after mating. Here, we provide evidence using oligonucleotide-directed affinity purification that all of the E.crassus telomerase complexes contain at least two enzyme active sites. Furthermore, we show using co-immunoprecipitation experiments that EcTERT, the telomerase catalytic subunit, undergoes multimerization in vitro. Two independent interaction domains were identified in EcTERT, one at the N-terminus that spans amino acids 186-354 and one at the C-terminu

SUBMITTER: Wang L 

PROVIDER: S-EPMC137098 | biostudies-literature | 2002 Sep

REPOSITORIES: biostudies-literature