Structural characterization of Spo0E-like protein-aspartic acid phosphatases that regulate sporulation in bacilli

Rosa Grenha, Neil J. Rzechorzek, James A. Brannigan, Rob N. de Jong, Eiso Ab, Tammo Diercks, Vincent Truffault, Joanne C. Ladds, Mark J. Fogg, Cristina Bongiorni, Marta Perego, Robert Kaptein, Keith S. Wilson, Gert E. Folkers, Anthony J. Wilkinson

Research output: Contribution to journalArticlepeer-review

Abstract

Spore formation is an extreme response of many bacterial species to starvation. In the case of pathogenic species of Bacillus and Clostridium, it is also a component of disease transmission. Entry into the pathway of sporulation in Bacillus subtilis and its relatives is controlled by an expanded two-component system in which starvation signals lead to the activation of sensor kinases and phosphorylation of the master sporulation response regulator Spo0A. Accumulation of threshold concentrations of Spo0A similar to P heralds the commitment to sporulation. Countering the activities of the sensor kinases are phosphatases such as Spo0E, which dephosphorylate Spo0A similar to P and inhibit sporulation. Spo0E-like protein-aspartic acid-phosphate phosphatases, consisting of 50-90 residues, are conserved in sporeforming bacteria and unrelated in sequence to proteins of known structure. Here we determined the structures of the Spo0A similar to P phosphatases BA1655 and BA5174 from Bacillus anthracis using nuclear magnetic resonance spectroscopy. Each is composed of two anti-parallel alpha-helices flanked by flexible regions at the termini. The signature SQELD motif (SRDLD in BA1655) is situated in the middle of helix alpha 2 with its polar residues projecting outward. BA5174 is a monomer, whereas BA1655 is a dimer. The four-helix bundle structure in the dimer is reminiscent of the phosphotransferase Spo0B and the chemotaxis phosphatase CheZ, although in contrast to these systems, the subunits in BA1655 are in head-to-tail rather than head-to-head apposition. The implications of the structures for interactions between the phosphatases and their substrate Spo0A similar to P are discussed.

Original languageEnglish
Pages (from-to)37993-38003
Number of pages11
JournalJournal of Biological Chemistry
Volume281
Issue number49
DOIs
Publication statusPublished - 8 Dec 2006

Keywords

  • TRANSCRIPTION FACTOR SPO0A
  • TORSION ANGLE DYNAMICS
  • RESPONSE REGULATOR
  • MOLECULAR RECOGNITION
  • SUBTILIS SPORULATION
  • HISTIDINE KINASES
  • ESCHERICHIA-COLI
  • PHOSPHORELAY
  • ASSIGNMENT
  • MECHANISM

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