Flagellar Hook Protein from Salmonella SJ25

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1 JOURNAL OF BACrERIOLOGY, Jan. 1976, p Copyright 1976 American Society for Microbiology Vol. 125, No. 1 Printed in U.S.A. Flagellar Hook Protein from Salmonella SJ25 HIROAKI KAGAWA,* KATSUSHI OWARIBE, SHO ASAKURA, AND NORIKO TAKAHASHI Institute of Molecular Biology, Faculty of Science, Nagoya University, Nagoya, 464, Japan,* and Department of Biochemistry, Nagoya City University, School of Medicine, Nagoya, 467, Japan Received for publication 10 September 1975 From acid-disintegrated flagellar hooks of Salmonella SJ25 an immunochemically pure preparation of hook protein was obtained by column chromatography. The molecular weight of the protein determined by sodium dodecyl sulfate-gel electrophoresis was 43,000, whereas that of SJ25 flagellin was 56,000. The amino-terminal residue of the hook protein was determined to be seryl. The amino acid composition of the protein was determined, the results being very similar to that for an Escherichia coli hook protein reported by Silverman and Simon (1972). Within a wavelength range of 200 to 250 nm, our purified preparation of hook protein gave a circular dichroism spectrum with unusually small amplitudes, suggesting that the a-helix content of the protein was very low. A bacterial flagellum detached from an intact cell by shearing consists of a main helical filament composed of flagellin (a flagellin filament) and a hook at the proximal end (1). The two parts have entirely different antigenic specificities (2, 3, 9, 11), suggesting that the hook region is composed of a protein other than flagellin. Indeed, Silverman and Simon (16) and Hilmen et al. (7) showed, using normal and mutant strains of Escherichia coli, that the hook structure is composed of a protein with a molecular weight of 42,000, instead of flagellin. Although the isolation of hooks has been attempted (1, 2, 3, 9), complete removal of flagellin from hooks is difficult if normally flagellated bacterial strains are used. For example, Kagawa et al. (9) isolated hooks from Salmonella SJ25 flagella and prepared antiserum against the hooks; however, the antiserum contained antibody to flagellin filaments, which had to be absorbed with a purified preparation of flagellin filaments. In this paper we describe a procedure for obtaining an immunochemically pure preparation of hook protein from acid-disintegrated hooks and we also characterize this protein. MATERIALS AND METHODS Two-step disintegration of isolated flagella. Salmonella SJ25, which produce normal flagella with 1,2-antigen, was supplied by T. lino (Faculty of Science, University of Tokyo). From a 16-liter culture of the strain flagella, which had been washed twice with distilled water and centrifuged, were isolated as described previously (9). The flagella (about 1 g total) were then suspended in 100 ml of a medium containing 0.15 M NaCl and 0.01 M phosphate buffer (ph 7.0) and heated at 60 C for 15 min to disintegrate flagellin filaments. The heated suspension was centrifuged at 105,000 x g for 2 h (high-speed centrifugation) and separated into the supernatant fluid, containing monomeric flagellin, and the sedimented material which was rich in hooks (9). This material was dispersed in 20 ml of distilled water, and the ph of the suspension was lowered to 1.8 by the addition of 1 N HCl to disintegrate the hooks into protein molecules. After incubation at room temperature for 30 min, the insoluble material in the acidic solution was removed by high-speed centrifugation, and the supernatant fluid was dialyzed against 0.01 M tris(hydroxymethyl)aminomethane (Tris)-hydrochloride buffer (ph 8.2) overnight in the cold. When the sedimented, insoluble material was observed by electron microscopy, hooks were rarely encountered; therefore, disintegration of hooks by the acid treatment was fairly complete. Column chromatography. The dialyzed solution was applied to a diethylaminoethyl-cellulose column (0.9 by 10 cm) equilibrated with 0.01 M Tris-hydrochloride buffer (ph 8.2), and adsorbed proteins were eluted with a 100-ml 0 to 0.15 M NaCl linear gradient in the same buffer (18). This method was very useful for the separation of the hook protein and flagellin from SJ25 flagella. Immunochemical experiments. A 0.5-ml solution containing about 0.5 mg of hook protein was emulsified with an equal volume of complete Freund adjuvant and injected subcutaneously into a rabbit. Injections were repeated four times at 2-week intervals, and blood was collected 1 week after the last injection. Antiserum was prepared by the conventional method. Antisera against flagellin filaments and intact hooks, which had been obtained previously (9), were also used. Double-diffusion tests were carried out on 1% (wt/vol) agar gels containing 0.15 M NaCl, 0.02 M veronal buffer (ph 8.6), and 0.01% NaN. The reac- 68

2 VOL. 125, 1976 tion was allowed to take place overnight in the cold. Flagella-carrying hooks were treated with antiserum against hook protein or intact hooks, and the products were observed with an electron microscope as described previously (9). SDS-gel electrophoresis. To determine the molecular weight of hook protein, sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis was performed by the method of Weber and Osborn (20). Ultraviolet absorption and circular dichroism measurements. Ultraviolet absorption spectra were recorded using a Hitachi type 124 spectrophotometer. Circular dichroism was kindly measured by N. Imai (Faculty of Science, Nagoya University), using a Jasco ORD/UV-20 apparatus. Protein concentration. The concentration of hook protein was determined by the microbiuret method, with bovine serum albumin as a standard (8). The absorbance of hook protein at 278 nm was 0.510/1-cm path per mg of protein per ml. For flagellin, the corresponding coefficient was (19). Determination of amino acid composition and amino-terminal residues. Hook protein was hydrolyzed with 6 N HCl in an evacuated, sealed tube at 110 C for 24 or 72 h, and each hydrolysate was analyzed, by the method of Spackman et al. (17), with a Hitachi KLA-3B apparatus. Three independent analyses were carried out to obtain final results. Tyrosine and tryptophan were determined by the method of Edelhoch (4). To detect cysteine, the method of Moore (14) was employed. To determine the amino-terminal residue of hook protein, the Edman degradation was used, with thinlayer chromatography for final identification of the phenylthiohydantoins (5). RESULTS Column chromatographic purification of hook protein. It is difficult to obtain intact hooks free from flagellin. However, if hooks are disintegrated by acid, hook protein can be separated from flagellin by column chromatography. Figure 1 shows an elution pattern in which the first peak corresponds to hook protein. This fraction was pooled for experiments. The second fraction was identified to be flagellin with 1,2-antigen, by immunodiffusion and SDS-gel electrophoresis (see below). The ratio in area between the first and second peaks changed to some extent depending upon the preparation of hooks. The last component, eluted with 3 M NaCl, was also 1,2-flagellin, as tested by immunodiffusion and SDS-gel electrophoresis. Suzuki and Iino (18) reported that, under a given set of chromatographic conditions, Salmonella flagellins with different antigenic specificities are eluted at different positions. SL23 is a strain that produces normal flagella with e,n,x-antigen. When we used flagella from SL23 as starting materials, hook SALMONELLA HOOK PROTEIN Fraction Number FIG. 1. Diethylaminoethyl-cellulose column chromatographic separation of SJ25 hook protein and flagellin. The total amount of protein applied to the column was about 10 mg. The last peak was eluted with 3 M NaCI. protein and flagellin were eluted at a position identical to that of the SJ25 hook protein. The yield of hook protein after the column chromatographic purification was 0.1 to 0.2% of the total amount of the flagella used. It should be noted that, if we use the data given by Abram et al. (1), the proportion of hook protein in the total weight of a flagellum is estimated to be 0.24% on the average. Immunodiffusion. The preparation of hook protein was tested by immunodiffusion whether or not it was still contaminated with flagellin. There were no cross-reactions between "hook protein" and flagellin (Fig. 2). That is, within the resolution resulting from the technique employed, our preparation of hook protein was pure. Moreover, between the "hook protein" and antiserum prepared against it, only a single precipitin band was formed, indicating that the antigens were possessed by a single kind of protein. Kagawa et al. (9) showed by electron microscopy that, when hook-carrying flagella were allowed to react toward antiserum specific to intact hooks, only the hook region of each flagellum was coated with antibody. The same result was obtained when hook-carrying flagella were treated with antiserum prepared against "hook protein." In this respect also, the protein was free from flagellin. In an immunodiffusion test, however, it was found that no precipitin band was formed between a purified preparation of hook protein and antiserum against hooks prepared in the previous study (9). The reason for this remains unknown. Determination of molecular weight. Upon SDS-gel electrophoresis, our preparation of hook protein gave a single band, which migrated about 20% faster than the band of

3 70 KAGAWA ET AL. J. BACTERIOL. rated. The values for tyrosine and tryptophan, determined by the method of Edelhoch (4), were 12.1 and 1.9, respectively; however, in Table 1 the value for tyrosine as determined by -p am - FIG. 2. Immunodiffusion pattern. (1) Antiserum against hook protein, (2) hook protein, (3) antiserum against flagellin filaments, and (4) flagellin. 1,2-flagellin (Fig. 3). The molecular weights of the hook protein and the flagellin determined by this method were 43,000 and 56,000, respectively (Fig. 4). The hook protein and a standard protein, ovalbumin, migrated at the same mobilities. When SL23 hooks were disintegrated by acid and the product was examined by SDS-gel electrophoresis, there was a dense band migrating at the same mobility as the SJ25 hook protein. Presumably, SL23 hook protein also has a molecular weight of 43,000. Amino-terminal residue. At the first step of the Edman degradation of a purified hook protein preparation, a single amino acid was released, which was identified as serine phenylthiohydantoins. Determination of the penultimate residue was unsuccessful. The amino-terminal residue of 1,2-flagellin has been identified to be alanyl (6, 12). Amino acid composition. Table 1 gives the results obtained in amino acid determinations of hook protein. The results are expressed as the number of amino acid residues per molecule, assuming a molecular weight of 43,000. The values for 24- and 72-h hydrolyses are averages of triplicate determinations. Cysteine was detected by a separate determination by the method of Moore (14). For valine and isoleucine, the data in the third column were adopted; the values for serine and threonine were determined by extrapolation to zero hydrolysis. It should be noted that, from the hydrolysates of hook protein, no unusual amino acids (such as N-methyl lysine and amino sugars) were sepaai c FIG. 3. SDS-gel electrophoretic pattern. (a) Hook protein, 10 Mg; (b) flagellin, 10,ug; and (c) hook protein, 10gg, plus flagellin, 10 g. 0 3: I Serum albumin a CGlobulin, H Ovalbumin Cytochrome C Mobility Chymotrypsin Globulin, L Myoglobin FIG. 4. Determination of the molecular weights of hook protein and flagellin by SDS-gel electrophoresis. The arrows a and b represent the mobilities of hook protein and flagellin, respectively. 1.2

4 VOL. 125, 1976 the amino acid analysis is given. In Table 2, the amino acid composition of hook protein thus determined is compared with that of 1,2-flagellin (6). Remarkable differences are: (i) hook TABLE 1. Amino acid Amino acid composition of SJ25 hook protein Amino acid residues (no./molecule) Avg or 24 ha 72 ha extrapolated value Lysine Histidine Arginine Aspartic acid Threonine Serine Glutamic acid Proline Glycine Alanine Cysteine 0 0 Valine Methionine Isoleucine Leucine Tyrosine Phenylalanine Tryptophan 1.9 a Hours of hydrolysis. TABLE 2. Amino acid compositions of SJ25 hook protein and flagellin Amino acid proteina Flagellin5 Lysine N-methyl lysine 0 13 Histidine 2 1 Arginine 6 15 Aspartic acid Threonine Serine Glutamic acid Proline 10 5 Glycine Alanine Cysteine 0 0 Valine Methionine 8 3 Isoleucine Leucine Tyrosine Phenylalanine 15 8 Tryptophan 2 0 a The number of amino acid residues per molecule of molecular weights 43,000. "The data are from reference 6. Number of amino acid residues per molecule of molecular weight 56,000. SALMONELLA HOOK PROTEIN 71 protein contains no N-methyl lysine, (ii) hook protein contains more aromatic amino acids than flagellin (tryptophan is absent in flagellin but present in hook protein), and (iii) hook protein contains more prolines than flagellin. Optical properties. Figure 5 compares ultraviolet absorption spectra for hook protein and flagellin. In the given wavelength range, the spectral curve for hook protein has considerably larger amplitudes than that for flagellin, since the former protein contains more aromatic amino acid residues than the latter. The difference in shape between the two spectral curves for wavelengths longer than 278 nm is largely due to the fact that tryptophan is absent in flagellin but present in hook protein. Our preparation of hook protein was found to have an unusual circular dichroism profile in the wavelength range 200 to 250 nm (Fig. 6). Although the mean residue molar ellipticity at 222 nm of 1,2-flagellin was about -9,000 degree cm2/dmol (19), the ellipticity at the same wavelength of hook protein was only one-ninth of this value. A straightforward interpretation of this result is that the a-helix content of the protein was very low. DISCUSSION In this paper we have shown that, when a crude preparation of Salmonella SJ25 hooks was incubated at ph 1.8 for complete disintegration, the product consisted of hook protein and flagellin, which could be separated by column chromatography. In fact, our preparation of hook protein was free from flagellin as tested by immunodiffusion. The molecular weight of the hook protein as determined by SDS-gel electrophoresis was 43,000, whereas that of the flagellin was 56,000. Silverman and Simon (16) showed, using "polyhooks" produced by a mutant strain of E. coli, that the subunit protein of the aberrant hooks had an SDS-gel electrophoretic mobility 20% larger than that of the E. coli flagellin. Also, Schmitt et al. (15) found, using complex flagella from Pseudomonas rhodos, that the molecular weight of the hook protein and flagellin was 43,000 and 55,000, respectively. These data are in good agreement with those reported here. Silverman and Simon (16) determined the amino acid composition of the subunit protein of E. coli polyhooks. The composition of the E. coli hook protein is very similar to that of Salmonella hook protein determined in this study. Let us represent the similarity in amino acid composition between two kinds of proteins in terms of difference index, DI (13). Then, if we

5 72 KAGAWA ET AL. ZO M n m FIG. 5. Ultraviolet absorption spectra from SJ25 hook protein and flagellin in the presence of 0.15 M NaCI-0.01 M Tris-hydrochloride buffer (ph 8.2) at room temperature. Solid curve, Hook protein (0.38 mg/ml); and dotted curve, flagellin (0.58 mg/ml). 0 x id FIG. 6. Circular dichroism spectra from hook protein (a) and flagellin (b) in the presence of 0.15 M NaCI-0.01 M Tris-hydrochloride buffer (ph 8.2) at 25 C. In both cases, the protein concentration was 0.5 mg/ml and the path length was 0.2 cm. use the data in Table 2 and those presented by Silverman and Simon (16), the value of DI for Salmonella and E. coli hook proteins is 5.0, whereas that for Salmonella and E. coli flagellins is 7.3. Table 2 gives a DI of 13.7 for hook protein and flagellin if N-methylation of lysines in the flagellin is disregarded. Our preparation of hook protein gave a circular dichroism spectrum with unusually small amplitudes between 200 and 250 nm. It is likely, therefore, that the a-helix content of the protein was very low. We must bear in mind the possibility that the a-helix content in the native J. BACTERIOL. state of the protein might have been destroyed irreversibly during the incubation at ph 1.8. In connection with this possibility, it is important to obtain a purified preparation of intact hooks and record its circular dichroism spectrum. This kind of experiment is now in progress. Finally, flagellin, which had been incubated at ph 1.8, was able to polymerize into helical filaments with the addition of seeds and gave a circular dichroism spectrum similar to that given in Fig. 6. ACKNOWLEDGMENTS We thank S. Takemura and M. Miyazaki of this Institute for helping with the column chromatographic experiments, and T. Hotta for assistance in the amino acid determination. LITERATURE CITED 1. Abram, D., J. R. Mitchen, H. Koffler, and A. E. Vatter Differentiation within the bacterial flagellum and isolation of the proximal hook. J. Bacteriol. 101: Dimmitt, K., and M. Simon Antigenic nature of bacterial flagellar hook structures. Infect. Immun. 1: Dimmitt, K., and M. Simon Purification and thermal stability of intact Bacillus subtilis flagella. J. Bacteriol. 105: Edelhoch, H Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6: Edman, P., and G. Begg A protein sequenator. Eur. J. Biochem. 1: Hotani, H., T. Ooi, H. Kagawa, S. Asakura, and S. Yamaguchi Biochemical evidence for identical primary structure of P-filament and flagellin. Biochim. Biophys. Acta 214: Hilmen, M., M. Silverman, and M. Simon The regulation of flagellar formation and function. J. Supramol. Biol. 2: Itzhaki, R. F., and D. M. Gill A micro-biuret method for estimating proteins. Anal. Biochem. 9: Kagawa, H., S. Asakura, and T. Iino Serological study of bacterial flagellar hooks. J. Bacteriol. 113: Konigsberg, W Substructive Edman degradation, p In C. H. W. Hirs (ed.), Methods in enzymology, vol. 11. Academic Press Inc., New York. 11. Lawn, A. W Simple immunological labelling method for electron microscopy and its application to the study of filamentous appendages of bacteria. Nature (London) 214: McDonough, M. W Amino acid composition of antigenically distinct Salmonella flagellar proteins. J. Mol. Biol. 12: Metzger, H., M. B. Shapiro, J. E. Mosimann, and J. E. Vinton Assessment of compositional relatedness between proteins. Nature (London) 219: Moore, S On the determination of cysteine as cysteic acid. J. Biol Chem. 238: Schmitt, R., I. Raska, and F. Mayer Plain and complex flagella of Pseudomonas rhodos: analysis of fine structure and composition. J. Bacteriol. 117: Silverman, M. R., and M. Simon Flagellar assembly mutants in Escherichia coli. J. Bacteriol. 112:

6 VOL. 125, Spackman, D. H., W. H. Stein, and S. Moore Automatic recording apparatus for use in the chromatography of amino acids. Anal. Chem. 30: Suzuki, H., and T. lino In vitro synthesis of phase-specific flagellin of Salmonella. J. Mol. Biol. 81: Uratani, Y., S. Asakura, and K. Imahori A circular SALMONELLA HOOK PROTEIN 73 dichroi4m study of Salmonella flagellin: evidence for conformational change on polymerization. J. Mol. Biol. 67:85-9A. 20. Weber, K., and M. Osborn The reliability of molecular weight determinations by dodecyl sulphatepolyacrylamide gel electrophoresis. J. Biol. Chem. 244:

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