Ontology highlight
ABSTRACT:
SUBMITTER: Chen Z
PROVIDER: S-EPMC5672036 | biostudies-literature | 2017 Nov
REPOSITORIES: biostudies-literature
The Journal of biological chemistry 20170906 44
The <i>de novo</i> assembly and post-splicing reassembly of the U4/U6.U5 tri-snRNP remain to be investigated. We report here that ZIP, a protein containing a CCCH-type zinc finger and a G-patch domain, as characterized by us previously, regulates pre-mRNA splicing independent of RNA binding. We found that ZIP physically associates with the U4/U6.U5 tri-small nuclear ribonucleoprotein (tri-snRNP). Remarkably, the ZIP-containing tri-snRNP, which has a sedimentation coefficient of ∼35S, is a tri-sn ...[more]