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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
14
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pubmed:dateCreated |
2009-8-11
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pubmed:databankReference |
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pubmed:abstractText |
Archaeal splicing endonucleases (EndAs) are currently classified into three groups. Two groups require a single subunit protein to form a homodimer or homotetramer. The third group requires two nonidentical protein components for the activity. To elucidate the molecular architecture of the two-subunit EndA system, we studied a crenarchaeal splicing endonuclease from Pyrobaculum aerophilum. In the present study, we solved a crystal structure of the enzyme at 1.7-A resolution. The enzyme adopts a heterotetrameric form composed of two catalytic and two structural subunits. By connecting the structural and the catalytic subunits of the heterotetrameric EndA, we could convert the enzyme to a homodimer that maintains the broad substrate specificity that is one of the characteristics of heterotetrameric EndA. Meanwhile, a deletion of six amino acids in a Crenarchaea-specific loop abolished the endonuclease activity even on a substrate with canonical BHB motif. These results indicate that the subunit architecture is not a major factor responsible for the difference of substrate specificity between single- and two-subunit EndA systems. Rather, the structural basis for the broad substrate specificity is built into the crenarchaeal splicing endonuclease itself.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-10331874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-10430568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-10986124,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-11060040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-11455964,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-11755525,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-11792869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-11842103,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-15109492,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-15299723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-15299926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-15572765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-15937113,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-15957218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-16039609,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-16219321,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-16221764,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-16330750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-1656050,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-16690865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-16781672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-17172768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-17495927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-17580114,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-17636125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-17827289,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-18156677,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-18217203,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-18711368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-18832079,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-2314256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-8460170,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-9200602,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-9200603,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-9200604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-9321408,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-9535656,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-9582290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19515941-9733681
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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 |
Aug
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pubmed:issn |
1362-4962
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4787-98
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pubmed:dateRevised |
2010-9-27
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pubmed:meshHeading |
pubmed-meshheading:19515941-Amino Acid Sequence,
pubmed-meshheading:19515941-Crystallography, X-Ray,
pubmed-meshheading:19515941-Endoribonucleases,
pubmed-meshheading:19515941-Models, Molecular,
pubmed-meshheading:19515941-Molecular Sequence Data,
pubmed-meshheading:19515941-Protein Engineering,
pubmed-meshheading:19515941-Protein Multimerization,
pubmed-meshheading:19515941-Protein Subunits,
pubmed-meshheading:19515941-Pyrobaculum,
pubmed-meshheading:19515941-Sequence Deletion,
pubmed-meshheading:19515941-Substrate Specificity
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pubmed:year |
2009
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pubmed:articleTitle |
Functional importance of crenarchaea-specific extra-loop revealed by an X-ray structure of a heterotetrameric crenarchaeal splicing endonuclease.
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pubmed:affiliation |
Department of Biomedical Chemistry, Graduate School of Medicine, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan. yoshinas@m.u-tokyo.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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