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Journal of Bacteriology, September 2006, p. 6396-6405, Vol. 188, No. 17
0021-9193/06/$08.00+0 doi:10.1128/JB.00249-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Kieran B. Pechter, and
Abraham L. Sonenshein*
Department of Molecular Biology and Microbiology, Tufts University School of Medicine, and Program in Molecular Microbiology, Sackler School of Graduate Biomedical Sciences, 136 Harrison Avenue, Boston, Massachusetts 02111
Received 17 February 2006/ Accepted 12 June 2006
Bacillus subtilis aconitase, encoded by the citB gene, is homologous to the bifunctional eukaryotic protein IRP-1 (iron regulatory protein 1). Like IRP-1, B. subtilis aconitase is both an enzyme and an RNA binding protein. In an attempt to separate the two activities of aconitase, the C-terminal region of the B. subtilis citB gene product was mutagenized. The resulting strain had high catalytic activity but was defective in sporulation. The defect was at a late stage of sporulation, specifically affecting expression of
K-dependent genes, many of which are important for spore coat assembly and require transcriptional activation by GerE. Accumulation of gerE mRNA and GerE protein was delayed in the aconitase mutant strain. Pure B. subtilis aconitase bound to the 3' untranslated region of gerE mRNA in in vitro gel mobility shift assays, strongly suggesting that aconitase RNA binding activity may stabilize gerE mRNA in order to allow efficient GerE synthesis and proper timing of spore coat assembly.
Present address: Department of Molecular and Cell Biology, University of California, Berkeley, CA 94270.
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