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Crystal structure of GerE, the ultimate transcriptional regulator of spore formation in Bacillus subtilis

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JournalJournal of Molecular Biology
DatePublished - 2 Mar 2001
Issue number4
Volume306
Number of pages13
Pages (from-to)759-771
Original languageEnglish

Abstract

The small, DNA-binding protein GerE regulates gene transcription in the terminally differentiated mother-cell compartment during late stages of sporulation in Bacillus subtilis. This versatile transcription factor shares sequence homology with the LuxR/FixJ/UhpA family of activators and modulates the expression of a number of genes, in particular those encoding the components of the coat that surrounds the mature spore. GerE orchestrates the final stages of coat deposition and maturation that lead to a spore with remarkable resistance properties but that must be responsive to low levels of germination signals. As this germination process is largely passive and can occur in the absence of de Move protein synthesis, the correct assembly of germination machinery, including germinant receptors and energy storage compounds, is crucial to the survival of the cell. The crystal structure of GerE has been solved at 2.05 Angstrom resolution using multi-wavelength anomalous dispersion techniques and reveals the nature of the GerE dimer. Each monomer comprises four a-helices, of which the central pair forms a helix-turn-helix DNA-binding motif. Implications for DNA-binding and the structural organisation of the LuxR/FixJ/UhpA family of transcription activator domains are discussed. (C) 2001 Academic Press.

    Research areas

  • bacillus, GerE, sporulation, transcription factor, X-ray crystallography, GENE-EXPRESSION, COAT PROTEIN, NUCLEOTIDE-SEQUENCE, SIGNAL-TRANSDUCTION, LAMBDA-REPRESSOR, BINDING DOMAIN, DNA, SPORULATION, GERMINATION, COMPLEX

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