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J Biol Chem, Vol. 273, Issue 20, 12109-12115, May 15, 1998

Characterization of the C-terminal Propeptide Involved in Bacterial Wall Spanning of -Amylase from the Psychrophile Alteromonas haloplanctis

Georges Feller, Salvino D'Amico, Abderrafi M. Benotmane, Fabian Joly, Jozef Van Beeumen^¶, and Charles Gerday

From the  Laboratory of Biochemistry, Institute of Chemistry B6, University of Liege, B-4000 Liege and the ^¶ Laboratory of Protein Biochemistry and Protein Engineering, University of Gent, B-9000 Gent, Belgium

The antarctic psychrophile Alteromonas haloplanctis secretes a Ca²⁺- and Cl-dependent -amylase. The nucleotide sequence of the amy gene and the amino acid sequences of the gene products indicate that the -amylase precursor is a preproenzyme composed by the signal peptide (24 residues), the mature -amylase (453 residues, 49 kDa), and a long C-terminal propeptide or secretion helper (192 residues, 21 kDa). In cultures of the wild-type strain, the 70-kDa precursor is secreted at the mid-exponential phase and is cleaved by a nonspecific protease into the mature enzyme and the propeptide. The purified C-terminal propeptide displays several features common to -pleated transmembrane proteins. It has no intramolecular chaperone function because active -amylase is expressed by Escherichia coli in the absence of the propeptide coding region. In E. coli, the 70-kDa precursor is directed toward the supernatant. When the -amylase coding region is excised from the gene, the secretion helper can still promote its own membrane spanning. It can also accept a foreign passenger, as shown by the extracellular routing of a -lactamase-propeptide fusion protein.

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