Reference - PMID:17559414 - Functional characterization of the phosphorelay protein Mpr1p from Schizosaccharomyces pombe.
Reference summary
- PubMed ID
- PMID:17559414
- Title
- Functional characterization of the phosphorelay protein Mpr1p from Schizosaccharomyces pombe.
- Authors
- Tan H, Janiak-Spens F, West AH
- Citation
- FEMS Yeast Res 2007 Sep;7(6):912-21
- Publication year
- 2007
- Abstract
- Histidine-containing phosphotransfer (HPt) proteins play an essential role in multistep histidine-aspartate phosphorelay signal transduction systems in prokaryotes and eukaryotes. The putative HPt protein in Schizosaccharomyces pombe, Mpr1p (also known as Spy1p), is a 295 amino acid protein that appears to be composed of more than one functional domain. The amino acid sequence of the N-terminal region of Mpr1p lacks homology to other known proteins, whereas the C-terminal domain is predicted to have structural similarity to the Ypd1p HPt protein from Saccharomyces cerevisiae. This study provides both in vitro and in vivo evidence that the C-terminal domain of Mpr1p indeed functions as an HPt protein in shuttling phosphoryl groups from one response regulator domain to another. Furthermore, we find that various deletions of the N-terminal region diminish both the phosphotransfer activity of Mpr1p and its affinity for response regulator domains, suggesting a possible role for the N-terminal domain in HPt-response regulator domain interactions.
