Source:http://linkedlifedata.com/resource/pubmed/id/19856287
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
2009-10-26
|
| pubmed:abstractText |
In order to identify functional residues of the bacteriophage SP6 RNA polymerase, its C-terminal one-twelfth region was randomly mutagenized using polymerase chain reactions of its gene under the conditions for reduced fidelity of Taq DNA polymerase. Using a two-vector system that permits phenotypic isolation of mutants with reduced in vivo transcription activity, 3 single and 1 multiple mutants were isolated. A single substitution of Gln for His805 resulted in complete inactivation of the enzyme. A multiple mutant carrying substitutions at 808, 820, 835, 843 and 848 also abolished the activity. However, changes of Pro856-->Ser and Asp862-->Glu individually reduced the activity only slightly. It is noteworthy that His805 is one of the two motif-C residues that are absolutely conserved among all the DNA polymerases and monomeric RNA polymerases.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
1039-9712
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
42
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
711-6
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| pubmed:year |
1997
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| pubmed:articleTitle |
The histidine-805 in motif-C of the phage SP6 RNA polymerase is essential for its activity as revealed by random mutagenesis.
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| pubmed:affiliation |
Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Taejon, Korea.
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| pubmed:publicationType |
Journal Article
|