<i>Saccharomyces cerevisiae</i> Ecm2 modulates the catalytic steps of pre-mRNA splicing.

ABSTRACT: Genetic, biochemical, and structural studies have elucidated the molecular basis for spliceosome catalysis. Splicing is RNA catalyzed and the essential snRNA and protein factors are well-conserved. However, little is known about how nonessential components of the spliceosome contribute to the reaction and modulate the activities of the fundamental core machinery. Ecm2 is a nonessential yeast splicing factor that is a member of the Prp19-related complex of proteins. Cryo-electron microscopy (cryo-EM) structures have revealed that Ecm2 binds the U6 snRNA and is entangled with Cwc2, a factor previously found to promote a catalytically active conformation of the spliceosome. These structures also indicate that Ecm2 and the U2 snRNA likely form a transient interaction during 5' splice site (SS)

SUBMITTER: van der Feltz C 

PROVIDER: S-EPMC8051269 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature