Site-directed mutagenesis of the yeast PRP20/SRM1 gene reveals distinct activity domains in the protein product.

doi:10.1007/BF00279748

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Article

Site-directed mutagenesis of the yeast PRP20/SRM1 gene reveals distinct activity domains in the protein product.

Molecular & general genetics : MGG - 17 Oct 1994

Lee A, Clark K L, Fleischmann M, Aebi M, Clark M W

Abstract excerpt

Prp20/Srm1, a homolog of the mammalian protein RCC1 in Saccharomyces cerevisiae, binds to double-stranded DNA (dsDNA) through a multicomponent complex in vitro. This dsDNA-binding capability of the Prp20 complex has been shown to be cell-cycle dependent; affinity for dsDNA is lost during DNA replication. By analyzing a number of temperature sensitive (ts) prp20 alleles produced in vivo and in vitro, as well as...

Topics

Alleles
Amino Acid Sequence
Animals
Cell Cycle Proteins
DNA
DNA, Fungal
DNA-Binding Proteins
Fungal Proteins
GTP-Binding Proteins
Guanine Nucleotide Exchange Factors
Humans

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Monomeric GTP-Binding Proteins

Mutagenesis, Site-Directed

Nuclear Proteins

Protein Binding

Recombinant Proteins

Saccharomyces cerevisiae

Source

Open in PubMed

Identifiers

PMID: 7845357
DOI: 10.1007/BF00279748

Genes

RCC1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7845357-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Site-directed mutagenesis of the yeast PRP20/SRM1 gene reveals distinct activity domains in the protein product.PMID 7845357Read ↗

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