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RNA-cleaving 10-23 deoxyribozyme with a single amino acid-like functionality operates without metal ion cofactorsThis article is part of a themed issue on Biophosphates
A series of 10-23 deoxyribozymes ( D2-D9 ) containing single amino-acid-bearing nucleosides (thr 6 dA, hisam 6 dA, hisam 5 dU and ncmnm 5 dU) at positions 4, 5, 8 or 15 of the catalytic core was obtained by chemical synthesis. The deoxyribozymes were screened for their catalytic efficiency, and in t...
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creator | Smuga, Damian Majchrzak, Kinga Sochacka, Elzbieta Nawrot, Barbara |
description | A series of 10-23 deoxyribozymes (
D2-D9
) containing single amino-acid-bearing nucleosides (thr
6
dA, hisam
6
dA, hisam
5
dU and ncmnm
5
dU) at positions 4, 5, 8 or 15 of the catalytic core was obtained by chemical synthesis. The deoxyribozymes were screened for their catalytic efficiency, and in the presence of 1 mM Mg
2+
two of them, containing at position 8 either hisam
5
dU (
D8
) or ncmnm
5
dU (
D9
), were found to be RNA nucleases several times more active than their non-modified precursor. Moreover, in the magnesium-free TRIS or PIPES buffers, these enzymes were able to catalyze the cleavage of the phosphodiester bond located between the 5′-GpU-3′ sequence of the complementary RNA substrate. The cleavage reaction proceeded with the highest efficiency at pH > 7.
We identified protein-like modified deoxyribozymes 10-23, which in the presence of Mg
2+
ions are more active than their parent precursor and can operate in a magnesium-free systems. |
doi_str_mv | 10.1039/b9nj00705a |
format | article |
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D2-D9
) containing single amino-acid-bearing nucleosides (thr
6
dA, hisam
6
dA, hisam
5
dU and ncmnm
5
dU) at positions 4, 5, 8 or 15 of the catalytic core was obtained by chemical synthesis. The deoxyribozymes were screened for their catalytic efficiency, and in the presence of 1 mM Mg
2+
two of them, containing at position 8 either hisam
5
dU (
D8
) or ncmnm
5
dU (
D9
), were found to be RNA nucleases several times more active than their non-modified precursor. Moreover, in the magnesium-free TRIS or PIPES buffers, these enzymes were able to catalyze the cleavage of the phosphodiester bond located between the 5′-GpU-3′ sequence of the complementary RNA substrate. The cleavage reaction proceeded with the highest efficiency at pH > 7.
We identified protein-like modified deoxyribozymes 10-23, which in the presence of Mg
2+
ions are more active than their parent precursor and can operate in a magnesium-free systems.</description><identifier>ISSN: 1144-0546</identifier><identifier>EISSN: 1369-9261</identifier><identifier>DOI: 10.1039/b9nj00705a</identifier><language>eng</language><creationdate>2010-05</creationdate><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Smuga, Damian</creatorcontrib><creatorcontrib>Majchrzak, Kinga</creatorcontrib><creatorcontrib>Sochacka, Elzbieta</creatorcontrib><creatorcontrib>Nawrot, Barbara</creatorcontrib><title>RNA-cleaving 10-23 deoxyribozyme with a single amino acid-like functionality operates without metal ion cofactorsThis article is part of a themed issue on Biophosphates</title><description>A series of 10-23 deoxyribozymes (
D2-D9
) containing single amino-acid-bearing nucleosides (thr
6
dA, hisam
6
dA, hisam
5
dU and ncmnm
5
dU) at positions 4, 5, 8 or 15 of the catalytic core was obtained by chemical synthesis. The deoxyribozymes were screened for their catalytic efficiency, and in the presence of 1 mM Mg
2+
two of them, containing at position 8 either hisam
5
dU (
D8
) or ncmnm
5
dU (
D9
), were found to be RNA nucleases several times more active than their non-modified precursor. Moreover, in the magnesium-free TRIS or PIPES buffers, these enzymes were able to catalyze the cleavage of the phosphodiester bond located between the 5′-GpU-3′ sequence of the complementary RNA substrate. The cleavage reaction proceeded with the highest efficiency at pH > 7.
We identified protein-like modified deoxyribozymes 10-23, which in the presence of Mg
2+
ions are more active than their parent precursor and can operate in a magnesium-free systems.</description><issn>1144-0546</issn><issn>1369-9261</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid/><recordid>eNqFj8FOwzAQRC0EEqVw4Y60fIDBbtpUOQIC9cQB9R5tnQ1ZcGLLdoDwRXwmBiFxg9M-7ezMaIU41epCq6K63FXDk1JrtcI9MdNFWclqUer9zHq5lGq1LA_FUYz5Rut1qWfi4-H-ShpL-MLDI2glFwU05N6mwDv3PvUEr5w6QIhZtwTY8-AADTfS8jNBOw4msRvQcprAeQqYKH6b3Jigp4QWsg7GtWiSC3HbcQQMiXMrZPSZwbW5InXUU5N3cSTIlmt2vnPRd1-Rx-KgRRvp5GfOxdnd7fZmI0M0tQ_cY5jq3_eLuTj_S6990xb_ZXwCKIpsvQ</recordid><startdate>20100501</startdate><enddate>20100501</enddate><creator>Smuga, Damian</creator><creator>Majchrzak, Kinga</creator><creator>Sochacka, Elzbieta</creator><creator>Nawrot, Barbara</creator><scope/></search><sort><creationdate>20100501</creationdate><title>RNA-cleaving 10-23 deoxyribozyme with a single amino acid-like functionality operates without metal ion cofactorsThis article is part of a themed issue on Biophosphates</title><author>Smuga, Damian ; Majchrzak, Kinga ; Sochacka, Elzbieta ; Nawrot, Barbara</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-rsc_primary_b9nj00705a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Smuga, Damian</creatorcontrib><creatorcontrib>Majchrzak, Kinga</creatorcontrib><creatorcontrib>Sochacka, Elzbieta</creatorcontrib><creatorcontrib>Nawrot, Barbara</creatorcontrib></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Smuga, Damian</au><au>Majchrzak, Kinga</au><au>Sochacka, Elzbieta</au><au>Nawrot, Barbara</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>RNA-cleaving 10-23 deoxyribozyme with a single amino acid-like functionality operates without metal ion cofactorsThis article is part of a themed issue on Biophosphates</atitle><date>2010-05-01</date><risdate>2010</risdate><volume>34</volume><issue>5</issue><spage>934</spage><epage>948</epage><pages>934-948</pages><issn>1144-0546</issn><eissn>1369-9261</eissn><abstract>A series of 10-23 deoxyribozymes (
D2-D9
) containing single amino-acid-bearing nucleosides (thr
6
dA, hisam
6
dA, hisam
5
dU and ncmnm
5
dU) at positions 4, 5, 8 or 15 of the catalytic core was obtained by chemical synthesis. The deoxyribozymes were screened for their catalytic efficiency, and in the presence of 1 mM Mg
2+
two of them, containing at position 8 either hisam
5
dU (
D8
) or ncmnm
5
dU (
D9
), were found to be RNA nucleases several times more active than their non-modified precursor. Moreover, in the magnesium-free TRIS or PIPES buffers, these enzymes were able to catalyze the cleavage of the phosphodiester bond located between the 5′-GpU-3′ sequence of the complementary RNA substrate. The cleavage reaction proceeded with the highest efficiency at pH > 7.
We identified protein-like modified deoxyribozymes 10-23, which in the presence of Mg
2+
ions are more active than their parent precursor and can operate in a magnesium-free systems.</abstract><doi>10.1039/b9nj00705a</doi><tpages>15</tpages></addata></record> |
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source | Royal Society of Chemistry Journals |
title | RNA-cleaving 10-23 deoxyribozyme with a single amino acid-like functionality operates without metal ion cofactorsThis article is part of a themed issue on Biophosphates |
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