snRNP公司
小核RNA
核糖核蛋白
核糖核酸
细胞生物学
RNA结合蛋白
化学
Prp24型
小核核糖核蛋白
生物
绑定域
分子生物学
作者
Sunbin Liu,Ping Li,Olexandr Dybkov,Stephanie Nottrott,Klaus Hartmuth,Reinhard Lührmann,Teresa Carlomagno,Markus C. Wahl
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2007-04-06
卷期号:316 (5821): 115-120
被引量:112
标识
DOI:10.1126/science.1137924
摘要
Although highly homologous, the spliceosomal hPrp31 and the nucleolar Nop56 and Nop58 (Nop56/58) proteins recognize different ribonucleoprotein (RNP) particles. hPrp31 interacts with complexes containing the 15.5K protein and U4 or U4atac small nuclear RNA (snRNA), whereas Nop56/58 associate with 15.5K–box C/D small nucleolar RNA complexes. We present structural and biochemical analyses of hPrp31-15.5K-U4 snRNA complexes that show how the conserved Nop domain in hPrp31 maintains high RNP binding selectivity despite relaxed RNA sequence requirements. The Nop domain is a genuine RNP binding module, exhibiting RNA and protein binding surfaces. Yeast two-hybrid analyses suggest a link between retinitis pigmentosa and an aberrant hPrp31-hPrp6 interaction that blocks U4/U6-U5 tri-snRNP formation.
科研通智能强力驱动
Strongly Powered by AbleSci AI