SpringerImages - ChiB products of the start codon mutants. ABPU/AP1 (wild type), B11/pyroA (ΔchiB), B11/chiB, B11/mutM1 and B11/mutM2 strains were grown in YG medium for indicated days, and cell extracts and culture supernatants were analyzed by Western blot experiment with the anti-ChiB antibody. One microgram of total protein from cell extracts or 1 μl of culture supernatant was loaded on each lane

ChiB products of the start codon mutants. ABPU/AP1 (wild type), B11/pyroA (ΔchiB), B11/chiB, B11/mutM1 and B11/mutM2 strains were grown in YG medium for indicated days, and cell extracts and culture supernatants were analyzed by Western blot experiment with the anti-ChiB antibody. One microgram of total protein from cell extracts or 1 μl of culture supernatant was loaded on each lane

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Fig 2

ChiB products of the start codon mutants. ABPU/AP1 (wild type), B11/pyroA (ΔchiB), B11/chiB, B11/mutM1 and B11/mutM2 strains were grown in YG medium for indicated days, and cell extracts and culture supernatants were analyzed by Western blot experiment with the anti-ChiB antibody. One microgram of total protein from cell extracts or 1 μl of culture supernatant was loaded on each lane

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The production of ChiB in these strains was analyzed by Western blot analysis using the anti-ChiB polyclonal antibody (Fig. 2 ).

The quantity of ChiB produced in the B11/mutM1 strain was nearly the same as that in the control strain B11/chiB ( Materials and methods ), whereas ChiB was not detected in the B11/mutM2 strain (Fig. 2 ).

Indeed, we found high levels of the enzymatically active protein in the culture medium (Fig. 3 ), but the determination of the initiation codon revealed that ChiB lacks the hydrophobic N-terminal region upstream of M2 (Figs. 1 , 2 ), a sequence that could function as a respective secretion signal.

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