MSL5 cDNA ORF clone, Saccharomyces cerevisiae S288C

The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.
Johnston M, Hillier L, Riles L, Albermann K, Andr? B, Ansorge W, Benes V, Br?ckner M, Delius H, Dubois E, D?sterh?ft A, Entian KD, Floeth M, Goffeau A, Hebling U, Heumann K, Heuss-Neitzel D, Hilbert H, Hilger F, Kleine K, K?tter P, Louis EJ, Messenguy F, Mewes HW, Hoheisel JD
Nature387(6632 Suppl)87-90(1997 May)

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

We also identify interfacial mutations in Msl5 that bypass the essentiality of Sub2, a DExD-box ATPase implicated in displacing Msl5 from the branchpoint in exchange for the U2 snRNP
Title: Structural basis for recognition of intron branchpoint RNA by yeast Msl5 and selective effects of interfacial mutations on splicing of yeast pre-mRNAs.

The results suggest a network of important but functionally buffered protein-protein and protein-RNA interactions between the Mud2-Msl5 complex at the branchpoint and the U1 snRNP at the 5' splice site.
Title: Structure-function analysis and genetic interactions of the yeast branchpoint binding protein Msl5.

a conserved zinc knuckle of the branch point-binding protein plays a different role in RNA processing than enhancing the binding of branch point-binding protein to the branch point sequence
Title: An extended RNA binding site for the yeast branch point-binding protein and the role of its zinc knuckle domains in RNA binding.