Effect of Proteolytic Enzymes on Bacterial Flagella

Author:

Martinez Rafael J.1,Shaper Joel H.1,Lundh Nancy P.1,Bernard Patricia D.1,Glazer A. N.1

Affiliation:

1. Instituto de Investigaciones Biomédicas, University of Mexico, Mexico 20, D. F.; Department of Bacteriology and Department of Biological Chemistry, University of California, Los Angeles, California 90024

Abstract

Sheared flagella of Salmonella typhimurium strains SL 870 (Nml + Fla + ) and SL 871 (Nml Fla + ) were found to be susceptible to proteolytic digestion by trypsin, chymotrypsin, and Pronase. The rate of tryptic digestion was similar for the ε- N -methyllysine-containing and the nonmethylated flagella. Thin fibers, which appeared to originate from only one end of the flagellar filament, were formed upon trypsin digestion. The fibers were not dissociated at extremes of p H or upon heating. The amino acid composition of the purified fibers was very different from that of intact Salmonella flagellin, and the fibers did not cross-react with antiflagellin or antiflagellar antiserum. The possible significance of these findings is discussed in relation to the flagellar structure.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference18 articles.

1. e-N-Methyl-lysine in bacterial flagella protein;Ambler R. P.;Nature (London),1959

2. The hydrolysis of two E-N-methyl-L-lysine derivatives by trypsin;Benoiton L.;Biochim. Biophys. Acta,1966

3. Champness J. N. and J. Lowy. 1968. The structure of bacterial flagella p. 106-114. In Symposium on fibrous proteins Australia 1967. Plenum Press New York N.Y.

4. Bacterial flagella: polarity of elongation;Emerson S. U.;Science,1970

5. Extraordinary polymerization of Salmonella flagellin in vitro;Hotani H.;Biochim. Biophys. Acta,1969

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