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PMID: 8925926 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Characterization of the newly constructed domains that replace P5abc within the Tetrahymena ribozyme.

FEBS letters ·Vol. 394 ·No. 1 ·1996-09-23 ·Pages 5-8

Ikawa Y, Shiraishi H, Inoue T

Abstract

The P5abc domain of the Tetrahymena ribozyme has been shown to function as an activator that enhances core catalytic activity of the ribozyme. We reported previously that several new domains in that their primary sequences are different from that of P5abc are also capable of activating the ribozyme. It was unclear whether the mechanism of activation by the new domains is identical to that by P5abc. We have investigated structural and functional properties of the new domains and obtained evidence that strongly indicates that a particular domain activates the ribozyme in a different manner from that by P5abc.

MeSH Terms
Adenine/metabolism Animals Base Sequence Dimethyl Sulfoxide/pharmacology Electrophoresis, Polyacrylamide Gel Enzyme Activation Introns Models, Genetic Molecular Sequence Data Mutagenesis Nucleic Acid Conformation Polymerase Chain Reaction RNA/chemistry,metabolism RNA, Catalytic/chemistry,genetics,metabolism Tetrahymena/genetics Transcription, Genetic
Chemicals
RNA, Catalytic RNA Adenine Dimethyl Sulfoxide
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Ikawa Y
Department of Chemistry, Faculty of Science, Kyoto University, Japan.
Shiraishi H
Inoue T
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1996-09-23
Pages
5-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
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