Document Detail


Nucleobase catalysis in the hairpin ribozyme.
MedLine Citation:
PMID:  16601203     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
RNA catalysis is important in the processing and translation of RNA molecules, yet the mechanisms of catalysis are still unclear in most cases. We have studied the role of nucleobase catalysis in the hairpin ribozyme, where the scissile phosphate is juxtaposed between guanine and adenine bases. We show that a modified ribozyme in which guanine 8 has been substituted by an imidazole base is active in both cleavage and ligation, with ligation rates 10-fold faster than cleavage. The rates of both reactions exhibit bell-shaped dependence on pH, with pK(a) values of 5.7 +/- 0.1 and 7.7 +/- 0.1 for cleavage and 6.1 +/- 0.3 and 6.9 +/- 0.3 for ligation. The data provide good evidence for general acid-base catalysis by the nucleobases.
Authors:
Timothy J Wilson; Jonathan Ouellet; Zheng-Yun Zhao; Shinya Harusawa; Lisa Araki; Takushi Kurihara; David M J Lilley
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-04-06
Journal Detail:
Title:  RNA (New York, N.Y.)     Volume:  12     ISSN:  1355-8382     ISO Abbreviation:  RNA     Publication Date:  2006 Jun 
Date Detail:
Created Date:  2006-05-24     Completed Date:  2006-07-12     Revised Date:  2010-09-15    
Medline Journal Info:
Nlm Unique ID:  9509184     Medline TA:  RNA     Country:  United States    
Other Details:
Languages:  eng     Pagination:  980-7     Citation Subset:  IM    
Affiliation:
Cancer Research UK Nucleic Acid Structure Research Group, The University of Dundee.
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MeSH Terms
Descriptor/Qualifier:
Adenosine / chemistry,  metabolism
Base Sequence
Binding Sites
Catalysis
Guanosine / chemistry,  metabolism
Hydrogen-Ion Concentration
Imidazoles / chemistry,  metabolism
Models, Molecular
Molecular Sequence Data
Nucleic Acid Conformation
RNA, Catalytic / chemistry*,  metabolism
Chemical
Reg. No./Substance:
0/Imidazoles; 0/RNA, Catalytic; 0/hairpin ribozyme; 118-00-3/Guanosine; 288-32-4/imidazole; 58-61-7/Adenosine
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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