| Title: | Pentapeptide regulation of aspartyl-phosphate phosphatases |
| Address: | "Division of Cellular Biology, Department of Molecular and Experimental Medicine, MEM-116, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. mperego@scripps.edu" |
| DOI: | 10.1016/s0196-9781(01)00490-9 |
| ISSN/ISBN: | 0196-9781 (Print) 0196-9781 (Linking) |
| Abstract: | "Aspartyl-phosphate phosphatases are integral components of the phosphorelay signal transduction system for sporulation initiation in Bacillus subtilis. The Rap and Spo0E families of protein phosphatases specifically dephosphorylate the sporulation response regulators Spo0F and Spo0A, respectively. The phosphatases interpret regulatory signals antithetical to sporulation and the Rap phosphatases are subject to inactivation by specific pentapeptides generated from an inactive peptide precursor. Additional regulatory signals are brought about by the complex activation circuit that generates the Phr pentapeptide inhibitors of Rap phosphatases. Phr peptide's recognition of the Rap phosphatase targets is remarkably specific. Specificity is dictated by the amino acid sequence of the pentapeptide. The identification of tetratricopeptide repeats in the Rap proteins may explain the mechanism by which Phr peptides bind to and inhibit the activity of Rap phosphatases" |
| Keywords: | Amino Acid Sequence Bacillus subtilis/*physiology Bacterial Proteins/*antagonists & inhibitors/drug effects Molecular Sequence Data Oligopeptides/*metabolism Pheromones/*metabolism Phosphoprotein Phosphatases/*antagonists & inhibitors *Sigma Factor Signal; |
| Notes: | "MedlinePerego, M Brannigan, J A eng GM 55594/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review 2001/10/06 Peptides. 2001 Oct; 22(10):1541-7. doi: 10.1016/s0196-9781(01)00490-9" |
