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The U11/U12 snRNP 65K protein acts as a molecular bridge, binding the U12 snRNA and U11-59K protein.
EMBO J. 2005 Sep 07; 24(17):3057-69.EJ

Abstract

U11 and U12 interact cooperatively with the 5' splice site and branch site of pre-mRNA as a stable preformed di-snRNP complex, thereby bridging the 5' and 3' ends of the intron within the U12-dependent prespliceosome. To identify proteins contributing to di-snRNP formation and intron bridging, we investigated protein-protein and protein-RNA interactions between components of the U11/U12 snRNP. We demonstrate that the U11/U12-65K protein possesses dual binding activity, interacting directly with U12 snRNA via its C-terminal RRM and the U11-associated 59K protein via its N-terminal half. We provide evidence that, in contrast to the previously published U12 snRNA secondary structure model, the 3' half of U12 forms an extended stem-loop with a highly conserved seven-nucleotide loop and that the latter serves as the 65K binding site. Addition of an oligonucleotide comprising the 65K binding site to an in vitro splicing reaction inhibited U12-dependent, but not U2-dependent, pre-mRNA splicing. Taken together, these data suggest that U11/U12-65K and U11-59K contribute to di-snRNP formation and intron bridging in the minor prespliceosome.

Authors+Show Affiliations

Department of Cellular Biochemistry, MPI of Biophysical Chemistry, Göttingen, Germany.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16096647

Citation

Benecke, Heike, et al. "The U11/U12 snRNP 65K Protein Acts as a Molecular Bridge, Binding the U12 snRNA and U11-59K Protein." The EMBO Journal, vol. 24, no. 17, 2005, pp. 3057-69.
Benecke H, Lührmann R, Will CL. The U11/U12 snRNP 65K protein acts as a molecular bridge, binding the U12 snRNA and U11-59K protein. EMBO J. 2005;24(17):3057-69.
Benecke, H., Lührmann, R., & Will, C. L. (2005). The U11/U12 snRNP 65K protein acts as a molecular bridge, binding the U12 snRNA and U11-59K protein. The EMBO Journal, 24(17), 3057-69.
Benecke H, Lührmann R, Will CL. The U11/U12 snRNP 65K Protein Acts as a Molecular Bridge, Binding the U12 snRNA and U11-59K Protein. EMBO J. 2005 Sep 7;24(17):3057-69. PubMed PMID: 16096647.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The U11/U12 snRNP 65K protein acts as a molecular bridge, binding the U12 snRNA and U11-59K protein. AU - Benecke,Heike, AU - Lührmann,Reinhard, AU - Will,Cindy L, Y1 - 2005/08/11/ PY - 2004/07/26/received PY - 2005/07/13/accepted PY - 2005/8/13/pubmed PY - 2005/10/26/medline PY - 2005/8/13/entrez SP - 3057 EP - 69 JF - The EMBO journal JO - EMBO J VL - 24 IS - 17 N2 - U11 and U12 interact cooperatively with the 5' splice site and branch site of pre-mRNA as a stable preformed di-snRNP complex, thereby bridging the 5' and 3' ends of the intron within the U12-dependent prespliceosome. To identify proteins contributing to di-snRNP formation and intron bridging, we investigated protein-protein and protein-RNA interactions between components of the U11/U12 snRNP. We demonstrate that the U11/U12-65K protein possesses dual binding activity, interacting directly with U12 snRNA via its C-terminal RRM and the U11-associated 59K protein via its N-terminal half. We provide evidence that, in contrast to the previously published U12 snRNA secondary structure model, the 3' half of U12 forms an extended stem-loop with a highly conserved seven-nucleotide loop and that the latter serves as the 65K binding site. Addition of an oligonucleotide comprising the 65K binding site to an in vitro splicing reaction inhibited U12-dependent, but not U2-dependent, pre-mRNA splicing. Taken together, these data suggest that U11/U12-65K and U11-59K contribute to di-snRNP formation and intron bridging in the minor prespliceosome. SN - 0261-4189 UR - https://www.unboundmedicine.com/medline/citation/16096647/The_U11/U12_snRNP_65K_protein_acts_as_a_molecular_bridge_binding_the_U12_snRNA_and_U11_59K_protein_ L2 - https://doi.org/10.1038/sj.emboj.7600765 DB - PRIME DP - Unbound Medicine ER -