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

Grenha R, Rzechorzek NJ, Brannigan JA, de Jong RN, Ab E, Diercks T, Truffault V, Ladds JC, Fogg MJ, Bongiorni C, Perego M, Kaptein R, Wilson KS, Folkers GE, Wilkinson AJ
J Biol Chem 281 37993-8003 (2006)
Cited: 10 times
EuropePMC logo PMID: 17001075

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 approximately P heralds the commitment to sporulation. Countering the activities of the sensor kinases are phosphatases such as Spo0E, which dephosphorylate Spo0A approximately 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 approximately 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 alpha2 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 approximately P are discussed.

Articles - 2bzb mentioned but not cited (1)

  1. Simultaneous prediction of protein folding and docking at high resolution. Das R, André I, Shen Y, Wu Y, Lemak A, Bansal S, Arrowsmith CH, Szyperski T, Baker D. Proc. Natl. Acad. Sci. U.S.A. 106 18978-18983 (2009)


Reviews citing this publication (2)

  1. Molecular Mechanisms of Two-Component Signal Transduction. Zschiedrich CP, Keidel V, Szurmant H. J. Mol. Biol. 428 3752-3775 (2016)
  2. Auxiliary phosphatases in two-component signal transduction. Silversmith RE. Curr. Opin. Microbiol. 13 177-183 (2010)

Articles citing this publication (7)

  1. Identical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrate. Pazy Y, Motaleb MA, Guarnieri MT, Charon NW, Zhao R, Silversmith RE. Proc. Natl. Acad. Sci. U.S.A. 107 1924-1929 (2010)
  2. Negative regulation of Bacillus anthracis sporulation by the Spo0E family of phosphatases. Bongiorni C, Stoessel R, Perego M. J. Bacteriol. 189 2637-2645 (2007)
  3. Sporulation during growth in a gut isolate of Bacillus subtilis. Serra CR, Earl AM, Barbosa TM, Kolter R, Henriques AO. J. Bacteriol. 196 4184-4196 (2014)
  4. NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs. Jeong JH, Kim JS, Choi SS, Kim Y. Biophys. J. 110 423-430 (2016)
  5. Comparative genomic study of spo0E family genes and elucidation of the role of Spo0E in Bacillus anthracis. Dubey GP, Narayan A, Mattoo AR, Singh GP, Kurupati RK, Zaman MS, Aggarwal A, Baweja RB, Basu-Modak S, Singh Y. Arch. Microbiol. 191 241-253 (2009)
  6. Molecular mechanism of the smart attack of pathogenic bacteria on nematodes. Zhang L, Wei Y, Tao Y, Zhao S, Wei X, Yin X, Liu S, Niu Q. Microb Biotechnol 13 683-705 (2020)
  7. The Transcription Factor CpcR Determines Cell Fate by Modulating the Initiation of Sporulation in Bacillus thuringiensis. Hou S, Zhang R, Lereclus D, Peng Q, Zhang J, Slamti L, Song F. Appl Environ Microbiol 88 e0237421 (2022)


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