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Pentapeptide regulation of aspartyl-phosphate phosphatases

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JournalPeptides
DatePublished - Oct 2001
Issue number10
Volume22
Number of pages7
Pages (from-to)1541-1547
Original languageEnglish

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. (C) 2001 Elsevier Science Inc. All rights reserved.

    Research areas

  • PROTEIN-PROTEIN INTERACTIONS, COMPLETE GENOME SEQUENCE, BACILLUS-SUBTILIS, BACTERIAL DEVELOPMENT, RESPONSE REGULATOR, STRUCTURAL BASIS, REPEAT PROTEINS, SNAP HELIX, PEPTIDE, TPR

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