Ontology highlight
ABSTRACT:
SUBMITTER: Pauling MH
PROVIDER: S-EPMC110834 | biostudies-literature | 2000 Mar
REPOSITORIES: biostudies-literature
Pauling M H MH McPheeters D S DS Ares M M
Molecular and cellular biology 20000301 6
To explore the dynamics of snRNP structure and function, we have studied Cus1p, identified as a suppressor of U2 snRNA mutations in budding yeast. Cus1p is homologous to human SAP145, a protein present in the 17S form of the human U2 snRNP. Here, we define the Cus1p amino acids required for function in yeast. The segment of Cus1p required for binding to Hsh49p, a homolog of human SAP49, is contained within an essential region of Cus1p. Antibodies against Cus1p coimmunoprecipitate U2 snRNA, as we ...[more]