Crystal structure of a eukaryotic group II intron lariat.
Crystal structure of a eukaryotic group II intron lariat.
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DOI:
10.1038/nature13790
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发表时间:
2014-10-09
期刊:
影响因子:
64.8
通讯作者:
Toor, Navtej
中科院分区:
文献类型:
--
作者:
Robart, Aaron R.;Chan, Russell T.;Peters, Jessica K.;Rajashankar, Kanagalaghatta R.;Toor, Navtej
The formation of branched lariat RNA is an evolutionarily conserved feature of splicing reactions for both group II and spliceosomal introns. The lariat is important for the fidelity of 5′ splice site selection and consists of a 2′-5′ phosphodiester bond between a bulged adenosine and the 5′ end of the intron. To gain insight into this ubiquitous intramolecular linkage, we determined the crystal structure of a eukaryotic group IIB intron in the lariat form at 3.7 Å. This revealed that two tandem tetraloop-receptor interactions, η-η’ and π-π’, place domain VI in the core to position the lariat bond in the post-catalytic state. Based on structural and biochemical data, we propose that π-π’ is a dynamic interaction that mediates the transition between the two steps of splicing, with η-η’ serving an ancillary role. The structure also reveals a four-magnesium-ion cluster involved in both catalysis and positioning of the 5′ end. Given the evolutionary relationship between group II and nuclear introns, it is likely that this active site configuration exists in the spliceosome as well.
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作者:
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通讯作者:
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DOI:
10.1107/s0907444904019158
发表时间:
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发表时间:
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期刊:
Acta crystallographica. Section D, Biological crystallography
影响因子:
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作者:
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通讯作者:
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