Direct involvement of the TEN domain at the active site of human telomerase

Jurczyluk, Julie, Nouwens, Amanda S., Holien, Jessica K., Adams, Timothy E., Lovrecz, George O., Parker, Michael W., Cohen, Scott B. and Bryan, Tracy M. (2011) Direct involvement of the TEN domain at the active site of human telomerase. Nucleic Acids Research, 39 5: 1774-1788. doi:10.1093/nar/gkq1083


Author Jurczyluk, Julie
Nouwens, Amanda S.
Holien, Jessica K.
Adams, Timothy E.
Lovrecz, George O.
Parker, Michael W.
Cohen, Scott B.
Bryan, Tracy M.
Title Direct involvement of the TEN domain at the active site of human telomerase
Journal name Nucleic Acids Research   Check publisher's open access policy
ISSN 0305-1048
1362-4962
Publication date 2011-03
Year available 2010
Sub-type Article (original research)
DOI 10.1093/nar/gkq1083
Open Access Status DOI
Volume 39
Issue 5
Start page 1774
End page 1788
Total pages 15
Place of publication Oxford, England
Publisher Oxford University Press
Collection year 2012
Language eng
Abstract Telomerase is a ribonucleoprotein that adds DNA to the ends of chromosomes. The catalytic protein subunit of telomerase (TERT) contains an N-terminal domain (TEN) that is important for activity and processivity. Here we describe a mutation in the TEN domain of human TERT that results in a greatly increased primer Kd, supporting a role for the TEN domain in DNA affinity. Measurement of enzyme kinetic parameters has revealed that this mutant enzyme is also defective in dNTP polymerization, particularly while copying position 51 of the RNA template. The catalytic defect is independent of the presence of binding interactions at the 50-region of the DNA primer, and is not a defect in translocation rate. These data suggest that the TEN domain is involved in conformational changes required to position the 30-end of the primer in the active site during nucleotide addition, a function which is distinct from the role of the TEN domain in providing DNA binding affinity.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes First published online: November 3, 2010

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2012 Collection
School of Chemistry and Molecular Biosciences
 
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Created: Wed, 09 Feb 2011, 14:59:37 EST by Dr Amanda Nouwens on behalf of Aust Institute for Bioengineering & Nanotechnology