作者: Piotr Wysoczanski , Markus Zweckstetter
DOI: 10.1080/15476286.2015.1096484
关键词:
摘要: One of the great challenges to structural biologists lies in explaining complexities spliceosome - a ribosome-sized molecular machine that is assembled step-wise manner and responsible for pre-mRNA splicing. The both fascinating difficult work with, because its dynamic nature. At each discrete step splicing tens proteins come go orchestrating functional transition through massive rearrangements. retention complex (RES) an important factor interacting with at onset first transesterification reaction. RES specific number genes controlling nucleus. 71 kDa heterotrimer composed 3 Pml1p, Bud13p Snu17p. We solved 3-dimensional structure core as well 2 dimers, Snu17p-Bud13p Snu17p-Pml1p. Further biophysical analysis revealed astounding cooperativity governs assembly this trimeric interaction pre-mRNA. more than 100-fold originates from progressive rigidification Snu17p upon coupled binding-and-folding protein regions, which are disordered unbound state. Our highlights role poses new questions about spliceosome.