Telomerase from Saccharomyces cerevisiae contains several protein subunits and may have different activities depending on the protein content.
Telomerase is a ribonucleoprotein responsible for maintaining telomeres during the cell cycle [1,2]. Here we describe a two-step purification procedure for the Saccharomyces cerevisiae telomerase complex. We have found that the properties (processivity, nuclease activity) of telomerase depend on the isolation procedure. Using a cross-linking approach, we have revealed several proteins that could be components of the telomerase complex. Furthermore, spectra of cross-linked proteins differ in processive and non-processive telomerase complexes.
Department of Chemistry, Moscow State University, Russia.
A V
AV
Petrov
S S
SS
Dokudovskaya
K A
KA
Sokolov
O I
OI
Lavrik
A
A
Favre
O A
OA
Dontsova
A A
AA
Bogdanov
D016375:Antisense Elements (Genetics); D002853:Chromatography, Liquid / Q000379:methods; D003432:Cross-Linking Reagents; D017931:DNA Primers / Q000737:chemistry / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism*; D008956:Models, Chemical; D012091:Repetitive Sequences, Nucleic Acid; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D019098:Telomerase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D014461:Ultracentrifugation
D016375:Antisense Elements (Genetics); D003432:Cross-Linking Reagents; D017931:DNA Primers; D005656:Fungal Proteins; D019098:Telomerase