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J Biol Chem, Vol. 273, Issue 41, 26455-26461, October 9, 1998
Identification and Characterization of the RNA Chaperone
Activity of Hepatitis Delta Antigen Peptides
Zhi-Shun
Huang and
Huey-Nan
Wu
From the Institute of Molecular Biology, Academia Sinica,
Taipei 11529, Taiwan, Republic of China
In this study, we identified an activity of the
hepatitis delta antigen that both modulates the cis-cleaving activities
of hepatitis delta virus (HDV) genomic RNA fragments and facilitates the trans-cleavage reactions between hammerhead ribozymes and the
cognate substrates of various lengths in vitro. Hepatitis delta antigen peptides exert their effect by accelerating the unfolding
and refolding of RNA molecules and by promoting strand annealing and
strand dissociation. In addition, the stimulatory effect of hepatitis
delta antigen peptide on hammerhead catalysis is observed whether the
peptide is removed or not by phenol/chloroform extraction prior to the
initiation of trans-cleavage reaction. Therefore, hepatitis delta
antigen peptide acts as an RNA chaperone. The RNA chaperone domain of
hepatitis delta antigen overlaps with the coiled-coil domain that is
rich in lysine residues. The RNA binding domains of hepatitis delta
antigen previously identified are not required for the RNA chaperone
activity identified herein. The RNA chaperone activity of hepatitis
delta antigen may be important for the regulation of HDV replication
in vivo.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.
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