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Science 12 May 2006:
Vol. 312. no. 5775, pp. 906 - 910
DOI: 10.1126/science.1126629

Reports

RNA Recognition and Cleavage by a Splicing Endonuclease

Song Xue, Kate Calvin, Hong Li*

The RNA splicing endonuclease cleaves two phosphodiester bonds within folded precursor RNAs during intron removal, producing the functional RNAs required for protein synthesis. Here we describe at a resolution of 2.85 angstroms the structure of a splicing endonuclease from Archaeglobus fulgidus bound with a bulge-helix-bulge RNA containing a noncleaved and a cleaved splice site. The endonuclease dimer cooperatively recognized a flipped-out bulge base and stabilizes sharply bent bulge backbones that are poised for an in-line RNA cleavage reaction. Cooperativity arises because an arginine pair from one catalytic domain sandwiches a nucleobase within the bulge cleaved by the other catalytic domain.

Department of Chemistry and Biochemistry, Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA.

* To whom correspondence should be addressed. E-mail: hongli{at}sb.fsu.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Y. K. Kim, K. Mizutani, K.-H. Rhee, K.-H. Nam, W. H. Lee, E. H. Lee, E. E. Kim, S.-Y. Park, and K. Y. Hwang (2007)
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The dawn of dominance by the mature domain in tRNA splicing.
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'In-line attack' conformational effect plays a modest role in an enzyme-catalyzed RNA cleavage: a free energy simulation study.
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Sequence-specific binding of single-stranded RNA: is there a code for recognition?.
S. D. Auweter, F. C. Oberstrass, and F. H.-T. Allain (2006)
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Science. ISSN 0036-8075 (print), 1095-9203 (online)