Cooperative Structure of the Heterotrimeric pre-mRNA Retention and Splicing Complex
Increased sodium tolerance protein 3, U2 snRNP protein SNU17
Bud site selection protein 13, Complexed with CEF1 protein 26, Synthetic lethal with CLF1 protein 7
GAMGNEYKDNAYIYIGNLNRELTEGDILTVFSEYGVPVDVILSRDENTGESQGFAYLKYEDQRSTILAVDNLNGFKIGGR ALKIDHTFYRPKRSLQKYYEAVKEELDRDIVSKNNAEK
AUTHORS STATE THAT THE ISOTOPICALLY LABELLED BIOSYNTHETIC PEPTIDES HAVE GS CLONING ARTIFACT AT THE N-TERMINI, WHICH WERE USED PRIMARILY TO DERIVE THE DATA THAT LEAD TO THE RELEVANT PARTS OF THE STRUCTURE. HOWEVER, THE NATURAL ISOTOPIC ABUNDANCE SYNTHETIC PEPTIDES WERE ALSO USED FOR SOME NMR EXPERIMENTS. THEY DO NOT HAVE GS CLONING ARTIFACT. INSTEAD, THEY HAVE ACETYL GROUP AT THE N-TERMINUS AND AMIDE AT THE C-TERMINUS.
25 mM sodium phosphate, 250 mM NaCl, 1 mM sodium azide, 0.9-1.3 mM [U-13C; U-15N] Snu17p, 1.1-1.5 mM Bud13p, 1.4-1.9 mM Pml1p, 90% H2O/10% D2O
25 mM sodium phosphate, 250 mM NaCl, 1 mM sodium azide, 1.0-1.3 mM Snu17p, 1.2-1.5 mM Bud13p, 0.8-1.0 mM [U-13C; U-15N] Pml1p, 90% H2O/10% D2O
25 mM sodium phosphate, 250 mM NaCl, 1 mM sodium azide, 1.0-1.3 mM Snu17p, 0.8-1.0 mM [U-10% 13C; U-99% 15N] Bud13p, 1.5-1.9 mM Pml1p, 90% H2O/10% D2O
25 mM sodium phosphate, 250 mM NaCl, 1 mM sodium azide, 0.9-1.3 mM [U-13C; U-15N; U-2H] Snu17p, 1.1-1.5 mM Bud13p, 1.4-1.9 mM Pml1p, 90% H2O/10% D2O
Brunger, Adams, Clore, Gros, Nilges and Read
Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
spliceosome, Snu17p, Bud13p, Pml1p, heterotrimer, cooperativity, RES, splicing, RRM, PROTEIN BINDING, Ist3p
NEYKDNAYIYIGNLNRELTEGDILTVFSEYGVPVDVILSRDENTGESQGFAYLKYEDQRSTILAVDNLNGFKIGGRALKI DHTFYRPKRSLQKYYEAVKEELDRDIVSKNNAEK