Abstract
SRP1, a suppressor of certain temperature-sensitive mutations in RNA polymerase I in Saccharomyces cerevisiae, encodes a protein that is associated with nuclear pores. By using a system of conditional SRP1 expression and by isolating temperature-sensitive srp1 mutants, we have demonstrated that Srp1p is essential for maintenance of the crescent-shaped nucleolar structure, RNA transcription, and the proper functions of microtubules as inferred from analysis of nuclear division/segregation and immunofluorescence microscopy of microtubules. Different mutant alleles showed significantly different phenotypes in relation to these apparently multiple functional roles of the protein. We have also found that eight imperfect 42-amino-acid tandem repeats present in Srp1p are similar to the 42-amino-acid repeats in armadillo/plakoglobin/beta-catenin proteins present in adhesive junction complexes of higher eukaryotes. We discuss this similarity in connection with the observed pleiotropic effects of srp1 mutations.
MeSH Terms
Amino Acid Sequence
Animals
Armadillo Domain Proteins
Cell Nucleolus/ultrastructure
Cell Nucleus/physiology,ultrastructure
Cytoskeletal Proteins/genetics
Desmoplakins
Drosophila Proteins
Microtubules/metabolism
Molecular Sequence Data
Mutation
Nuclear Proteins/genetics,physiology
Proteins/genetics
RNA Polymerase I/metabolism
Repetitive Sequences, Nucleic Acid
Saccharomyces cerevisiae/genetics,physiology,ultrastructure
Sequence Homology, Amino Acid
Trans-Activators
Transcription, Genetic
alpha Karyopherins
beta Catenin
gamma Catenin
Chemicals
Armadillo Domain Proteins
Cytoskeletal Proteins
Desmoplakins
Drosophila Proteins
Nuclear Proteins
Proteins
Trans-Activators
alpha Karyopherins
beta Catenin
gamma Catenin
RNA Polymerase I
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Yano R
Department of Biological Chemistry, University of California, Irvine 91717-1700.
Oakes M L
Tabb M M
Nomura M
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