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Unité de Physiologie Cellulaire and URA 1300 CNRS, Département des Biotechnologies, Institut Pasteur, 28 rue du Dr Roux, 75724 Paris Cedex 15, France
Station de Microscopie Electronique, Institut Pasteur, 28 rue du Dr Roux, 75724 Paris Cedex 15, France
ABSTRACT
Summary: The protomer forming the S-layer of Clostridium thermocellum was identified as a 140 kDa protein which was non-covalently bound to the cell wall. Cloning and sequencing of the corresponding gene revealed an open reading frame of 3108 nucleotides encoding a polypeptide of 1036 amino acids, termed SIpA. The amino acid composition of SIpA matches the composition of a previously described exocellular glycoprotein. SIpA shared extensive similarity with the S-layer protein of Bacillus sphaericus and with the outer wall protein of Bacillus brevis. In addition, the amino-terminal region of SIpA contained a segment presenting similarities with segments termed SLH (S-layer homologous), which are found in several bacterial exoproteins. A polypeptide of 209 residues comprising this segment was shown to bind to cell walls extracted from C. thermocellum cells.
Author for correspondence: Pierre Béguin. Tel: +33 1 45 68 88 19. Fax: + 33 1 45 68 87 90. e-mail: beguin@pasteur.fr
Present address: Département de Biochimie Médicale, Centre Médical Universitaire, 1 rue Michel Servet, CH-1211 Geneva 4, Switzerland.
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