2009年8月
Functional importance of Crenarchaea-specific extra-loop revealed by an X-ray structure of a heterotetrameric crenarchaeal splicing endonuclease
NUCLEIC ACIDS RESEARCH
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- 巻
- 37
- 号
- 14
- 開始ページ
- 4787
- 終了ページ
- 4798
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1093/nar/gkp506
- 出版者・発行元
- OXFORD UNIV PRESS
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.
- リンク情報
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- DOI
- https://doi.org/10.1093/nar/gkp506
- CiNii Articles
- http://ci.nii.ac.jp/naid/80020499539
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/19515941
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000269015400023&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1093/nar/gkp506
- ISSN : 0305-1048
- eISSN : 1362-4962
- CiNii Articles ID : 80020499539
- PubMed ID : 19515941
- Web of Science ID : WOS:000269015400023