Reciprocal regulation of nuclear import of the yeast MutSα DNA mismatch repair proteins Msh2 and Msh6
| Autor: | Mark D. Rose, Leah A. Sevi, Alison E. Gammie, Alicia P. Hayes, Megan C. Feldt |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Cytoplasm
congenital hereditary and neonatal diseases and abnormalities Saccharomyces cerevisiae Proteins DNA Repair DNA repair Green Fluorescent Proteins Immunoblotting Active Transport Cell Nucleus Saccharomyces cerevisiae Biology Biochemistry Article Two-Hybrid System Techniques medicine NLS Fluorescent Antibody Technique Indirect neoplasms Molecular Biology Cell Nucleus MutS Homolog 2 Protein nutritional and metabolic diseases Cell Biology Molecular biology digestive system diseases Cell biology DNA-Binding Proteins Protein Transport Cell nucleus medicine.anatomical_structure MSH3 MSH2 Mutagenesis Site-Directed Nuclear transport Nuclear localization sequence |
| Zdroj: | DNA Repair. 8:739-751 |
| ISSN: | 1568-7864 |
| DOI: | 10.1016/j.dnarep.2009.02.003 |
| Popis: | DNA mismatch recognition is performed in eukaryotes by two heterodimers known as MutSalpha (Msh2/Msh6) and MutSbeta (Msh2/Msh3) that must reside in the nucleus to function. Two putative Msh2 nuclear localization sequences (NLS) were characterized by fusion to green fluorescent protein (GFP) and site-directed mutagenesis in the context of Msh2. One NLS functioned in GFP targeting assays and both acted redundantly within Msh2. We examined nuclear localization of each of the MutS monomers in the presence and absence of their partners. Msh2 translocated to the nucleus in cells lacking Msh3 and Msh6; however, cells lacking Msh6 showed significantly decreased levels of nuclear Msh2. Furthermore, the overall protein levels of Msh2 were significantly diminished in the absence of Msh6, particularly if Msh2 lacked a functional NLS. Msh3 localized in the absence of Msh2, but Msh6 localization depended on Msh2 expressing functional NLSs. Overall, the nuclear levels of Msh2 and Msh6 decline when the other partner is absent. The data suggest a stabilization mechanism to prevent free monomer accumulation in the cytoplasm. |
| Databáze: | OpenAIRE |
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