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PMID: 9305980 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Identification of determinants for inhibitor binding within the RNA active site of human telomerase using PNA scanning.

Biochemistry ·Vol. 36 ·No. 39 ·1997-09-30 ·Pages 11873-80

Hamilton SE, Pitts AE, Katipally RR, Jia X, Rutter JP, Davies BA, Shay JW, Wright WE, Corey DR

Abstract

Telomerase is a ribonucleoprotein that participates in the maintenance of telomere length. Its activity is up-regulated in many tumor types, suggesting that it may be a novel target for chemotherapy. The RNA component of telomerase contains an active site that plays at least two roles&sbd;binding telomere ends and templating their replication [Greider, C. W., & Blackburn, E. H. (1989) Nature 337, 331-337]. The accessibility of RNA nucleotides for inhibitor binding cannot be assumed because of the potential for RNA secondary structure and RNA-protein interactions. Here we use high-affinity recognition by overlapping peptide nucleic acids (PNAs) [Nielsen, P. E., et al. (1991) Science 254, 1497-1500] to identify nucleotides within the RNA active site of telomerase that are determinants for inhibitor recognition. The IC50 for inhibition decreases from 30 microM to 10 nM as cytidines 50-52 (C50-52) at the boundary between the alignment and elongation domains are recognized by PNAs overlapping from the 5' direction. As C50-52 are uncovered in the 3' direction, IC50 increases from 10 nM to 300 nM. As cytidine 56 at the extreme 3' end of the active site is uncovered, IC50 values increase from 0.5 microM to 10 microM. This analysis demonstrates that C50-C52 and C56 are important for PNA recognition and are physically accessible for inhibitor binding. We use identification of these key determinants to minimize the size of PNA inhibitors, and knowledge of these determinants should facilitate design of other small molecules capable of targeting telomerase. The striking differences in IC50 values for inhibition of telomerase activity by related PNAs emphasize the potential of PNAs to be sensitive probes for mapping complex nucleic acids. We also find that PNA hybridization is sensitive to nearest-neighbor interactions, and that consecutive guanine bases within a PNA strand increase binding to complementary DNA and RNA sequences.

MeSH Terms
Binding Sites Humans Oligodeoxyribonucleotides/pharmacology Peptides/pharmacology RNA/metabolism Telomerase/antagonists & inhibitors,metabolism Telomere/metabolism Templates, Genetic
Chemicals
Oligodeoxyribonucleotides Peptides RNA Telomerase
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Hamilton S E
Department of Pharmacology, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75235, USA.
Pitts A E
Katipally R R
Jia X
Rutter J P
Davies B A
Shay J W
Wright W E
Corey D R
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
1997-09-30
Pages
11873-80
Language
English
Region
United States
NLM ID
0370623
Subset
IM
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