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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
38
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pubmed:dateCreated |
2008-9-17
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pubmed:abstractText |
Methanothermobacter thermautotrophicus minichromosomal maintenance protein (mtMCM) is a 75 kDa protein that self-assembles into a double hexamer structure. The double hexamer formed by the N-terminal region of mtMCM has a highly charged (overwhelmingly net positive) inner channel. Here we investigate the effects of point mutations of some of these charged residues on the biological activities of mtMCM. Although all of the mutants were similar to the wild type in protein folding and complex assembly, we found that mutations impaired helicase activity. The study of the DNA binding and ATPase activities of these mutants revealed that the impairment of the helicase activity was highly correlated with a decrease in DNA binding, providing evidence consistent with the role of these charged residues of the inner channel in interactions with DNA.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18754676-10454994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18754676-10611290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18754676-10677495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18754676-10747908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18754676-10872463,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18754676-11282021,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18754676-12045100,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18754676-12548282,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18754676-12774115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18754676-15007098,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18754676-15100218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18754676-15342486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18754676-15454080,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18754676-16221679,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18754676-16242991,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18754676-9927482
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1520-4995
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
23
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pubmed:volume |
47
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9981-6
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pubmed:dateRevised |
2011-5-25
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pubmed:meshHeading |
pubmed-meshheading:18754676-Amino Acid Sequence,
pubmed-meshheading:18754676-Amino Acid Substitution,
pubmed-meshheading:18754676-Archaeal Proteins,
pubmed-meshheading:18754676-DNA Helicases,
pubmed-meshheading:18754676-DNA-Binding Proteins,
pubmed-meshheading:18754676-Methanobacteriaceae,
pubmed-meshheading:18754676-Molecular Sequence Data,
pubmed-meshheading:18754676-Point Mutation,
pubmed-meshheading:18754676-Protein Folding,
pubmed-meshheading:18754676-Protein Processing, Post-Translational
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pubmed:year |
2008
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pubmed:articleTitle |
Identification of amino acids important for the biochemical activity of Methanothermobacter thermautotrophicus MCM.
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pubmed:affiliation |
Molecular and Computational Biology, University of Southern California, Los Angeles, California 90089-2910, USA.
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pubmed:publicationType |
Journal Article
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