Nucleic Acids Research Advance Access published online on February 8, 2007
Nucleic Acids Research, doi:10.1093/nar/gkm011
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Ribosomal protein L20 controls expression of the Bacillus subtilis infC operon via a transcription attenuation mechanism
CNRS UPR9073, Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France
*To whom correspondence should be addressed. Tel: + 33 1 58 41 51 27; Fax: + 33 1 58 41 50 20; Email: putzer{at}ibpc.fr
Received October 5, 2006. Revised December 22, 2006. Accepted December 27, 2006.
In contrast to Escherichia coli no molecular mechanism controlling the biosynthesis of ribosomal proteins has been elucidated in Gram-positive organisms. Here we show that the expression of the Bacillus subtilis infC-rpmI-rplT operon encoding translation factor IF3 and the ribosomal proteins L35 and L20 is autoregulated by a complex transcription attenuation mechanism. It implicates a 200-bp leader region upstream of infC which contains two conserved regulatory elements, one of which can act as a transcription terminator. Using in vitro and in vivo approaches we show that expression of the operon is regulated at the level of transcription elongation by a change in the structure of the leader mRNA which depends upon the presence of ribosomal protein L20. L20 binds to a phylogenetically conserved domain and provokes premature transcription termination at the leader terminator. Footprint and toeprint experiments support a regulatory model involving molecular mimicry between the L20-binding sites on 23S rRNA and the mRNA. Our data suggest that Nomura's model of ribosomal protein biosynthesis based on autogenous control and molecular mimicry is also valid in Gram-positive organisms.
Present address: Sergine Even, UMR INRA 1253, Laboratoire de Microbiologie, 65 rue de Saint Brieuc, CS 84215, 35042 RENNES cedex, France