Divalent hammerhead ribozyme targeting template region of human telomerase RNA has potent cleavage activity, but less inhibitory activity on telomerase

2002 ◽  
Vol 405 (1) ◽  
pp. 32-37 ◽  
Author(s):  
Yasuhiro Yokoyama ◽  
Xiaoyun Wan ◽  
Yuichiro Takahashi ◽  
Ariyoshi Shinohara ◽  
Tang Liulin ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Hammerhead Ribozyme ◽  
Telomerase Rna ◽  
Cleavage Activity ◽  
Human Telomerase ◽  
Template Region

scholarly journals Structural features of mouse telomerase RNA are responsible for the lower activity of mouse telomerase versus human telomerase

2006 ◽  
Vol 397 (3) ◽  
pp. 399-406 ◽  
Author(s):  
Scott J. Garforth ◽  
Yan Yun Wu ◽  
Vinayaka R. Prasad
Keyword(s):  
Telomerase Activity ◽  
Structural Features ◽  
In Vitro Translation ◽  
Telomerase Rna ◽  
Level Of Activity ◽  
Human Telomerase ◽  
High Degree ◽  
Made In ◽  
Template Region

Human and mouse telomerases show a high degree of similarity in both the protein and RNA components. Human telomerase is more active and more processive than the mouse telomerase. There are two key differences between hTR [human TR (telomerase RNA)] and mTR (mouse TR) structures. First, the mouse telomerase contains only 2 nt upstream of its template region, whereas the human telomerase contains 45 nt. Secondly, the template region of human telomerase contains a 5-nt alignment domain, whereas that of mouse has only 2 nt. We hypothesize that these differences are responsible for the differential telomerase activities. Mutations were made in both the hTR and mTR, changing the template length and the length of the RNA upstream of the template, and telomerase was reconstituted in vitro using mouse telomerase reverse transcriptase generated by in vitro translation. We show that the sequences upstream of the template region, with a potential to form a double-stranded helix (the P1 helix) as in hTR, increase telomerase activity. The longer alignment domain increases telomerase activity only in the context of the P1 helix. Thus the TR contributes to regulating the level of activity of mammalian telomerases.

A cytometric assay for ultrasensitive and robust detection of human telomerase RNA based on toehold strand displacement

2017 ◽  
Vol 87 ◽  
pp. 1071-1076 ◽  
Author(s):  
Jing Xu ◽  
Yanjun Wang ◽  
Luzhu Yang ◽  
Yanfang Gao ◽  
Baoxin Li ◽  
...  
Keyword(s):  
Telomerase Rna ◽  
Strand Displacement ◽  
Robust Detection ◽  
Human Telomerase

scholarly journals Single-Molecule FRET Reveals the Folding Dynamics of the Human Telomerase RNA Pseudoknot Domain

2012 ◽  
Vol 51 (24) ◽  
pp. 5876-5879 ◽  
Author(s):  
Martin Hengesbach ◽  
Nak-Kyoon Kim ◽  
Juli Feigon ◽  
Michael D. Stone
Keyword(s):  
Single Molecule ◽  
Telomerase Rna ◽  
Single Molecule Fret ◽  
Folding Dynamics ◽  
Human Telomerase ◽  
Rna Pseudoknot

scholarly journals Telomerase Activity Reconstitutedin Vitrowith Purified Human Telomerase Reverse Transcriptase and Human Telomerase RNA Component

2000 ◽  
Vol 275 (29) ◽  
pp. 22568-22573 ◽  
Author(s):  
Kenkichi Masutomi ◽  
Shuichi Kaneko ◽  
Naoyuki Hayashi ◽  
Tatsuya Yamashita ◽  
Yukihiro Shirota ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Telomerase Activity ◽  
Telomerase Reverse Transcriptase ◽  
Telomerase Rna ◽  
Human Telomerase Reverse Transcriptase ◽  
Human Telomerase
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