Grenha, R., Rzechorzek, N.J., Brannigan, J.A., de Jong, R.N., Ab, E., Diercks, T., Truffault, V., Ladds, J.C., Fogg, M.J., Bongiorni, C., Perego, M., Kaptein, R., Wilson, K.S., Folkers, G.E. and Wilkinson, A.J. (2006) Structural characterisation of Spo0E-like protein aspartic acid phosphatases that regulate sporulation in Bacilli. Journal of Biological Chemistry, 281 (49). pp. 37993-38003. ISSN 0021-9258Full text not available from this repository.
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 Spo0AP heralds the commitment to sporulation. Countering the activities of the sensor kinases are phosphatases such as Spo0E, which dephosphorylate Spo0AP 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 Spo0AP 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 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 Spo0AP are discussed.
|Academic Units:||The University of York > Chemistry (York)|
|Depositing User:||York RAE Import|
|Date Deposited:||28 Apr 2009 14:45|
|Last Modified:||28 Apr 2009 14:45|
|Publisher:||The American Society for Biochemistry and Molecular Biology|
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