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Structural model of the p14/SF3b155 · branch duplex complex.

Schellenberg MJ, Dul EL, MacMillan AM
RNA 17 155-65 (2011)
Cited: 17 times
EuropePMC logo PMID: 21062891

Abstract

Human p14 (SF3b14), a component of the spliceosomal U2 snRNP, interacts directly with the pre-mRNA branch adenosine within the context of the bulged duplex formed between the pre-mRNA branch region and U2 snRNA. This association occurs early in spliceosome assembly and persists within the fully assembled spliceosome. Analysis of the crystal structure of a complex containing p14 and a peptide derived from p14-associated SF3b155 combined with the results of cross-linking studies has suggested that the branch nucleotide interacts with a pocket on a non-canonical RNA binding surface formed by the complex. Here we report a structural model of the p14 · bulged duplex interaction based on a combination of X-ray crystallography of an adenine p14/SF3b155 peptide complex, biochemical comparison of a panel of disulfide cross-linked protein-RNA complexes, and small-angle X-ray scattering (SAXS). These studies reveal specific recognition of the branch adenosine within the p14 pocket and establish the orientation of the bulged duplex RNA bound on the protein surface. The intimate association of one surface of the bulged duplex with the p14/SF3b155 peptide complex described by this model buries the branch nucleotide at the interface and suggests that p14 · duplex interaction must be disrupted before the first step of splicing.

Articles - 3lqv mentioned but not cited (4)

  1. Structural basis of branch site recognition by the human spliceosome. Tholen J, Razew M, Weis F, Galej WP. Science 375 50-57 (2022)
  2. Structural model of the p14/SF3b155 · branch duplex complex. Schellenberg MJ, Dul EL, MacMillan AM. RNA 17 155-165 (2011)
  3. The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins. Chakraborty S, Rendón-Ramírez A, Ásgeirsson B, Dutta M, Ghosh AS, Oda M, Venkatramani R, Rao BJ, Dandekar AM, Goñi FM. F1000Res 2 286 (2013)
  4. Structural and mechanistic insights into human splicing factor SF3b complex derived using an integrated approach guided by the cryo-EM density maps. Rakesh R, Joseph AP, Bhaskara RM, Srinivasan N. RNA Biol 13 1025-1040 (2016)


Reviews citing this publication (6)

  1. The significant other: splicing by the minor spliceosome. Turunen JJ, Niemelä EH, Verma B, Frilander MJ. Wiley Interdiscip Rev RNA 4 61-76 (2013)
  2. Structural insight into RNA recognition motifs: versatile molecular Lego building blocks for biological systems. Muto Y, Yokoyama S. Wiley Interdiscip Rev RNA 3 229-246 (2012)
  3. The role of splicing factor mutations in the pathogenesis of the myelodysplastic syndromes. Boultwood J, Dolatshad H, Varanasi SS, Yip BH, Pellagatti A. Adv Biol Regul 54 153-161 (2014)
  4. Group II intron lariat: Structural insights into the spliceosome. Peters JK, Toor N. RNA Biol 12 913-917 (2015)
  5. Splicing factor gene mutations in the myelodysplastic syndromes: impact on disease phenotype and therapeutic applications. Pellagatti A, Boultwood J. Adv Biol Regul 63 59-70 (2017)
  6. Structural and functional modularity of the U2 snRNP in pre-mRNA splicing. van der Feltz C, Hoskins AA. Crit. Rev. Biochem. Mol. Biol. 54 443-465 (2019)

Articles citing this publication (7)



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