An AU at the first base pair of helix 3 elevates the catalytic activity of hepatitis delta virus ribozymes

A mutational analysis of the helix 3 (H3) region of hepatitis delta virus (HDV) ribozymes disclosed that an AU at the first base pair of H3 elevates the catalytic activity of various cis- and trans-acting HDV ribozymes. A GC to AU substitution at this position of H3, which is located at the junction...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 1997-08, Vol.413 (2), p.299-303
Main Authors: Huang, Zhi-Shun, Ping, Yueh-Hsin, Wu, Huey-Nan
Format: Article
Language:English
Subjects:
Base Sequence - genetics
cis-Cleavage
Hepatitis delta virus (HDV) ribozyme
Hepatitis Delta Virus - enzymology
Hepatitis Delta Virus - genetics
Hydrogen-Ion Concentration
Molecular Sequence Data
Mutation
Nucleic Acid Conformation
Ribozyme
RNA, Catalytic - chemistry
RNA, Catalytic - metabolism
RNA, Viral - chemistry
RNA, Viral - metabolism
trans-Cleavage
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A mutational analysis of the helix 3 (H3) region of hepatitis delta virus (HDV) ribozymes disclosed that an AU at the first base pair of H3 elevates the catalytic activity of various cis- and trans-acting HDV ribozymes. A GC to AU substitution at this position of H3, which is located at the junction of three of the four helices of the pseudoknot-like structure model, altered the structure of HDV ribozymes. This substitution in the H3 did not change the independence of the cleavage rate to pH nor the sensitivity to formamide treatment of the ribozymes.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)00902-2