Yeast calmodulin and a conserved nuclear protein participate in the in vivo binding of a matrix association region

Barbara R. Fishel, Ann O. Sperry, And William T Garrard

Research output: Contribution to journalArticlepeer-review

36 Scopus citations

Abstract

Chromatin becomes reorganized during mitosis each cell cycle. To identify genes potentially involved in these supramolecular events, we have used a colony-color assay to screen temperature-sensitive mutants of Saccharomyces cerevisiae. When a sequence that mediates attachment to the nuclear matrix in vitro was inserted into the GAL1 promoter of a lacZ fusion gene, β-galactosidase synthesis was inhibited. This observation permitted screening for temperature-sensitive-inducible mutants on 5-bromo-4-chloro-3-indolyl β-D-galactoside plates. Only 1 of 20 complementation groups of newly isolated mutants exhibited temperature-sensitive inducibility for the matrix association region but not for control CEN3 or STE6 inserts - a cmd1 mutant in which the last 7 amino acids of calmodulin were truncated by an ochre termination codon. Another mutant (smi1) exhibited a rare phenotype at the nonpermissive condition, which included S phase and budding arrest. We cloned and sequenced the SMI1 gene, which encodes a 57-kDa polypeptide with evolutionary conserved epitope(s) found in mammalian cell nuclei. Thus, we provide evidence for involvement of calmodulin and another conserved protein in the in vivo binding of a matrix association region.

Original languageEnglish (US)
Pages (from-to)5623-5627
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume90
Issue number12
DOIs
StatePublished - Jun 15 1993

Keywords

  • Gene regulation
  • Nuclear matrix-scaffold
  • Scaffold-attached region

ASJC Scopus subject areas

  • General

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