MersV1, Istex, Corpus, bibRecord, 000443

Properties of Hepatitis Delta Virus Ribozyme, Which Consists of Three RNA Oligomer Strands

Identifieur interne : 000443 ( Istex/Corpus ); précédent : 000442; suivant : 000444

Properties of Hepatitis Delta Virus Ribozyme, Which Consists of Three RNA Oligomer Strands

Auteurs : Taiichi Sakamoto ; Yoichiro Tanaka ; Tomoko Kuwabara ; Mi Hee Kim ; Yasuyuki Kurihara ; Masato Katahira ; Seiichi Uesugi

Source :

The Journal of Biochemistry [ 0021-924X ] ; 1997.

RBID : ISTEX:B73C48192583C9E0912CB7E36FE7F92B8AF98A3A

Abstract

Properties of a hepatitis delta virus (HDV) RNA ribozyme system, which consists of three RNA oligomer strands (substrate 8-mer; enzyme 16-mer plus 35-mer) and contains a hybrid sequence of genomic and antigenomic RNA cores, are reported. Effects of Mg2+ concentration, divalent metal ion species, pH, and temperature on the cleavage activity were examined. The substrate cleavage activity increased with increasing Mg2+ concentration (0-100 mM). Ca2+ and Mn2+ ions were the most effective divalent cations and Mg2+ was less effective. The cleavage activity increased with increasing pH (5-7.5). The optimum temperature for the cleavage activity was 25–40°C. The Mg2+ concentration, pH and temperature dependencies are different from those reported for the single-strand ribozymes (about 90-mer) although the divalent metal ion preference is very similar. Conformational change induced by Mg2+ ion titration was monitored by CD. The CD data and the activity-Mg2+ concentration data were analyzed by curve-fitting analysis using equations derived for multiple metal ion binding mechanisms. The data can be explained by a model in which three Mg2+ ions bind to one ribozyme unit.

Url:

https://api.istex.fr/ark:/67375/HXZ-8KKSMDW9-1/fulltext.pdf

DOI: 10.1093/oxfordjournals.jbchem.a021704

Links to Exploration step

ISTEX:B73C48192583C9E0912CB7E36FE7F92B8AF98A3A

Le document en format XML

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<profileDesc><abstract><p>Properties of a hepatitis delta virus (HDV) RNA ribozyme system, which consists of three RNA oligomer strands (substrate 8-mer; enzyme 16-mer plus 35-mer) and contains a hybrid sequence of genomic and antigenomic RNA cores, are reported. Effects of Mg<hi rend="superscript">2+</hi>
 concentration, divalent metal ion species, pH, and temperature on the cleavage activity were examined. The substrate cleavage activity increased with increasing Mg<hi rend="superscript">2+</hi>
 concentration (0-100 mM). Ca<hi rend="superscript">2+</hi>
 and Mn<hi rend="superscript">2+</hi>
 ions were the most effective divalent cations and Mg<hi rend="superscript">2+</hi>
 was less effective. The cleavage activity increased with increasing pH (5-7.5). The optimum temperature for the cleavage activity was 25–40°C. The Mg<hi rend="superscript">2+</hi>
 concentration, pH and temperature dependencies are different from those reported for the single-strand ribozymes (about 90-mer) although the divalent metal ion preference is very similar. Conformational change induced by Mg<hi rend="superscript">2+</hi>
 ion titration was monitored by CD. The CD data and the activity-Mg<hi rend="superscript">2+</hi>
 concentration data were analyzed by curve-fitting analysis using equations derived for multiple metal ion binding mechanisms. The data can be explained by a model in which three Mg<hi rend="superscript">2+</hi>
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<article-title>Properties of Hepatitis Delta Virus Ribozyme, Which Consists of Three RNA Oligomer Strands<xref ref-type="fn" rid="fn1"><sup>1</sup>
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<contrib contrib-type="author">

<name><surname>Sakamoto</surname>
<given-names>Taiichi</given-names>
</name>

</contrib>

<contrib contrib-type="author">

<name><surname>Tanaka</surname>
<given-names>Yoichiro</given-names>
</name>

</contrib>

<contrib contrib-type="author">

<name><surname>Kuwabara</surname>
<given-names>Tomoko</given-names>
</name>

</contrib>

<contrib contrib-type="author">

<name><surname>Kim</surname>
<given-names>Mi Hee</given-names>
</name>

</contrib>

<contrib contrib-type="author">

<name><surname>Kurihara</surname>
<given-names>Yasuyuki</given-names>
</name>

</contrib>

<contrib contrib-type="author">

<name><surname>Katahira</surname>
<given-names>Masato</given-names>
</name>

</contrib>

<contrib contrib-type="author">

<name><surname>Uesugi</surname>
<given-names>Seiichi</given-names>
</name>
<xref ref-type="corresp" rid="cor1"><sup>2</sup>
</xref>

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<aff><institution>Department of Bioengineering, Faculty of Engineering, Yokohama National University</institution>
 <addr-line>79-5 Tokiwadai, Hodogayaku, Yokohama 240</addr-line>
</aff>

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<corresp id="cor1"><sup>2</sup>
To whom correspondence should be addressed. Phone/Fax: + 81.45.339.4265 E-mail: <email>uesugi@mac.bio.bsk.ynu.ac.jp</email>
</corresp>

<fn id="fn1"><p><sup>1</sup>
This research was supported in part by Grants-in-Aid for Scientific Research on Priority Areas (*05265211, *05244101, *06276103,*08249212, *08680715) from the Ministry of Education, Science, Sports and Culture of Japan and by the Proposal-Based Advanced Industrial Technology R&D Program from the New Energy and Industrial Technology Development Organization (NEDO) of Japan. M.K. was supported by grants from the Kanagawa Academy of Science and Technology and Kato Memorial Bioscience Foundation.</p>
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<month>1</month>

<year>1997</year>

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<copyright-statement>© 1997 BY THE JOURNAL OF BIOCHEMISTRY</copyright-statement>

<copyright-year>1997</copyright-year>

<abstract>

<p>Properties of a hepatitis delta virus (HDV) RNA ribozyme system, which consists of three RNA oligomer strands (substrate 8-mer; enzyme 16-mer plus 35-mer) and contains a hybrid sequence of genomic and antigenomic RNA cores, are reported. Effects of Mg<sup>2+</sup>
 concentration, divalent metal ion species, pH, and temperature on the cleavage activity were examined. The substrate cleavage activity increased with increasing Mg<sup>2+</sup>
 concentration (0-100 mM). Ca<sup>2+</sup>
 and Mn<sup>2+</sup>
 ions were the most effective divalent cations and Mg<sup>2+</sup>
 was less effective. The cleavage activity increased with increasing pH (5-7.5). The optimum temperature for the cleavage activity was 25–40°C. The Mg<sup>2+</sup>
 concentration, pH and temperature dependencies are different from those reported for the single-strand ribozymes (about 90-mer) although the divalent metal ion preference is very similar. Conformational change induced by Mg<sup>2+</sup>
 ion titration was monitored by CD. The CD data and the activity-Mg<sup>2+</sup>
 concentration data were analyzed by curve-fitting analysis using equations derived for multiple metal ion binding mechanisms. The data can be explained by a model in which three Mg<sup>2+</sup>
 ions bind to one ribozyme unit.</p>

</abstract>

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<kwd>hepatitis delta virus</kwd>

<kwd>metal binding</kwd>

<kwd>oligonucleotide</kwd>

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<abstract>Properties of a hepatitis delta virus (HDV) RNA ribozyme system, which consists of three RNA oligomer strands (substrate 8-mer; enzyme 16-mer plus 35-mer) and contains a hybrid sequence of genomic and antigenomic RNA cores, are reported. Effects of Mg2+ concentration, divalent metal ion species, pH, and temperature on the cleavage activity were examined. The substrate cleavage activity increased with increasing Mg2+ concentration (0-100 mM). Ca2+ and Mn2+ ions were the most effective divalent cations and Mg2+ was less effective. The cleavage activity increased with increasing pH (5-7.5). The optimum temperature for the cleavage activity was 25–40°C. The Mg2+ concentration, pH and temperature dependencies are different from those reported for the single-strand ribozymes (about 90-mer) although the divalent metal ion preference is very similar. Conformational change induced by Mg2+ ion titration was monitored by CD. The CD data and the activity-Mg2+ concentration data were analyzed by curve-fitting analysis using equations derived for multiple metal ion binding mechanisms. The data can be explained by a model in which three Mg2+ ions bind to one ribozyme unit.</abstract>
<note type="footnotes">1This research was supported in part by Grants-in-Aid for Scientific Research on Priority Areas (*05265211, *05244101, *06276103,*08249212, *08680715) from the Ministry of Education, Science, Sports and Culture of Japan and by the Proposal-Based Advanced Industrial Technology R&D Program from the New Energy and Industrial Technology Development Organization (NEDO) of Japan. M.K. was supported by grants from the Kanagawa Academy of Science and Technology and Kato Memorial Bioscience Foundation.</note>
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Properties of Hepatitis Delta Virus Ribozyme, Which Consists of Three RNA Oligomer Strands

Properties of Hepatitis Delta Virus Ribozyme, Which Consists of Three RNA Oligomer Strands

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