| Autor: |
Frank, Peter, Braunshofer-Reiter, Christa, Karwan, Anneliese, Grimm, Rudolf, Wintersberger, Ulrike |
| Zdroj: |
FEBS Letters; May 1999, Vol. 450 Issue: 3 p251-256, 6p |
| Abstrakt: |
We purified Saccharomyces cerevisiaeRNase H(70) to homogeneity, using an optimized chromatographic purification procedure. Renaturation gel assay assigned RNase H activity to a 70 kDa polypeptide. Sequencing of tryptic peptides identified the open reading frame YGR276c on chromosome VII of the S. cerevisiaegenome as the corresponding gene, which encodes a putative polypeptide of molecular mass of 62 849. We therefore renamed this gene RNH70. Immunofluorescence microscopy using a RNH70‐EGFP fusion construct indicates nuclear localization of RNase H(70). Deletion of RNH70from the yeast genome did not result in any serious phenotype under the conditions tested. Homology searches revealed striking similarity with a number of eukaryotic proteins and open reading frames, among them the chimpanzee GOR protein, a homolog of a human autoimmune antigen, found to elicit autoimmune response in patients infected with hepatitis C virus. |
| Databáze: |
Supplemental Index |
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