Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 12 May 2006:
Vol. 312. no. 5775, pp. 906 - 910
DOI: 10.1126/science.1126629
Prev | Table of Contents | Next

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

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Crystal structure and assembly of the functional Nanoarchaeum equitans tRNA splicing endonuclease.
M. Mitchell, S. Xue, R. Erdman, L. Randau, D. Soll, and H. Li (2009)
Nucleic Acids Res.
   Abstract »    Full Text »    PDF »
Functional importance of Crenarchaea-specific extra-loop revealed by an X-ray structure of a heterotetrameric crenarchaeal splicing endonuclease.
S. Yoshinari, T. Shiba, D.-K. Inaoka, T. Itoh, G. Kurisu, S. Harada, K. Kita, and Y.-i. Watanabe (2009)
Nucleic Acids Res.
   Abstract »    Full Text »    PDF »
Structure-activity relationships in Kluyveromyces lactis {gamma}-toxin, a eukaryal tRNA anticodon nuclease.
N. Keppetipola, R. Jain, B. Meineke, M. Diver, and S. Shuman (2009)
RNA 15, 1036-1044
   Abstract »    Full Text »    PDF »
Human RNA 5'-kinase (hClp1) can function as a tRNA splicing enzyme in vivo.
A. Ramirez, S. Shuman, and B. Schwer (2008)
RNA 14, 1737-1745
   Abstract »    Full Text »    PDF »
Mammalian 2',3' cyclic nucleotide phosphodiesterase (CNP) can function as a tRNA splicing enzyme in vivo.
B. Schwer, A. Aronova, A. Ramirez, P. Braun, and S. Shuman (2008)
RNA 14, 204-210
   Abstract »    Full Text »    PDF »
Identification and characterization of a tRNA decoding the rare AUA codon in Haloarcula marismortui.
C. Kohrer, G. Srinivasan, D. Mandal, B. Mallick, Z. Ghosh, J. Chakrabarti, and U. L. Rajbhandary (2008)
RNA 14, 117-126
   Abstract »    Full Text »    PDF »
Structural and Mutational Analysis of tRNA Intron-Splicing Endonuclease from Thermoplasma acidophilum DSM 1728: Catalytic Mechanism of tRNA Intron-Splicing Endonucleases.
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)
J. Bacteriol. 189, 8339-8346
   Abstract »    Full Text »    PDF »
The dawn of dominance by the mature domain in tRNA splicing.
G. D. Tocchini-Valentini, P. Fruscoloni, and G. P. Tocchini-Valentini (2007)
PNAS 104, 12300-12305
   Abstract »    Full Text »    PDF »
'In-line attack' conformational effect plays a modest role in an enzyme-catalyzed RNA cleavage: a free energy simulation study.
D. Min, S. Xue, H. Li, and W. Yang (2007)
Nucleic Acids Res.
   Abstract »    Full Text »    PDF »
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)
Nucleic Acids Res. 34, 4943-4959
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)