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 (+3 others)
2006 Journal of Biological Chemistry  
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
more » ... hold concentrations of Spo0AϳP heralds the commitment to sporulation. Countering the activities of the sensor kinases are phosphatases such as Spo0E, which dephosphorylate Spo0AϳP 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 Spo0AϳP phosphatases BA1655 and BA5174 from Bacillus anthracis using nuclear magnetic resonance spectroscopy. Each is composed of two anti-parallel ␣-helices flanked by flexible regions at the termini. The signature SQELD motif (SRDLD in BA1655) is situated in the middle of helix ␣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 chemo-*
doi:10.1074/jbc.m607617200 pmid:17001075 fatcat:yrsbgxqrnfgqrmhgfy4wzozi5m