Functional mammalian spliceosomal complex E contains SMN complex proteins in addition to U1 and U2 snRNPs.

ABSTRACT: Spliceosomes remove introns from primary gene transcripts. They assemble de novo on each intron through a series of steps that involve the incorporation of five snRNP particles and multiple non-snRNP proteins. In mammals, all the intermediate complexes have been characterized on one transcript (MINX), with the exception of the very first, complex E. We have purified this complex by two independent procedures using antibodies to either U1-A or PRPF40A proteins, which are known to associate at an early stage of assembly. We demonstrate that the purified complexes are functional in splicing using commitment assays. These complexes contain components expected to be in the E complex and a number of previously unrecognized factors, including survival of motor neurons (SMN) and proteins of the SM

SUBMITTER: Makarov EM 

PROVIDER: S-EPMC3315330 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature