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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1997-3-18
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pubmed:abstractText |
The catalytic mechanism for self-splicing of the group I intron in the pre-mRNA from the nrdB gene in bacteriophage T4 has been investigated using 2'-amino- 2'-deoxyguanosine or guanosine as cosubstrates in the presence of Mg2+, Mn2+and Zn2+. The results show that a divalent metal ion interacts with the cosubstrate and thereby influences the efficiency of catalysis in the first step of splicing. This suggests the existence of a metal ion that catalyses the nucleophilic attack of the cosubstrate. Of particular significance is that the transesterification reactions of the first step of splicing with 2'-amino-2'-deoxyguanosine as cosubstrate are more efficient in mixtures containing either Mn2+or Zn2+together with Mg2+than with only magnesium ions present. The experiments in metal ion mixtures show that two (or more) metal ions are crucial for the self-splicing of group I introns and suggest the possibility that more than one of these have a direct catalytic role. A working model for a two-metal-ion mechanism in the transesterification steps is suggested.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-1282238,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-1381347,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-1550590,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-1709734,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-2036355,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-2261475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-2470150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-2470151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-3422485,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-3530746,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-3639741,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-3757035,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-6562377,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-7683490,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-7688573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-8172903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-8341661,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-8357544,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-839306,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-8421499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-8422960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-8422972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-8494902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9016608-8665863
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2'-amino-2'-deoxyguanosine,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyguanosine,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleotide Reductases,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0305-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
648-53
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9016608-Bacteriophage T4,
pubmed-meshheading:9016608-Cations, Divalent,
pubmed-meshheading:9016608-Deoxyguanosine,
pubmed-meshheading:9016608-Guanosine,
pubmed-meshheading:9016608-Introns,
pubmed-meshheading:9016608-Magnesium,
pubmed-meshheading:9016608-Manganese,
pubmed-meshheading:9016608-RNA, Viral,
pubmed-meshheading:9016608-RNA Precursors,
pubmed-meshheading:9016608-RNA Splicing,
pubmed-meshheading:9016608-Ribonucleotide Reductases,
pubmed-meshheading:9016608-Substrate Specificity,
pubmed-meshheading:9016608-Viral Proteins,
pubmed-meshheading:9016608-Zinc
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pubmed:year |
1997
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pubmed:articleTitle |
Metal ion interaction with cosubstrate in self-splicing of group I introns.
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pubmed:affiliation |
Department of Molecular Biology, Arrhenius Laboratory, Stockholm University, S-10691 Stockholm, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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