Identification of two forms of the Eso1 protein in Schizosaccharomyces pombe.
Cell Biol Int
; 38(5): 682-8, 2014 May.
Article
em En
| MEDLINE
| ID: mdl-24375893
ABSTRACT
In Schizosaccharomyces pombe, Eso1p is a protein fusion. Two-thirds of its N-terminus is conserved to budding yeast Rad30, which functions in error-free replication of UV-damaged DNA. A third of the C-terminus is highly conserved to budding yeast Eco1, a lysine acetyltransferase, which is essential for the establishment of cohesion. Both Rad30p and Eco1p need to be finely tuned in budding yeast. Given the distinct function existed in Rad30p and Eco1p, it is enigmatic how the Eso1p, the protein fusion regulated in S. pombe, works. We have identified two forms of the Eso1 protein by Western blot, and detected the Eco1-homology fragment by M/S analysis following TAP purification of Eso1 protein. The result raises the possibility that Eso1 might be processed in vivo to release the Eco1-homology fragment, which allows the independent regulation of Rad30-homology and Eco1-homology fragments.
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Bases de dados:
MEDLINE
Assunto principal:
Schizosaccharomyces
/
Proteínas de Ciclo Celular
/
Proteínas de Schizosaccharomyces pombe
Tipo de estudo:
Diagnostic_studies
Idioma:
En
Revista:
Cell Biol Int
Ano de publicação:
2014
Tipo de documento:
Article
País de afiliação:
China