Summary
Flagellin molecules of Rhodopseudomonas palustris have a molecular weight of 15,500 when they are determined in the analytical ultracentrifuge. But when the method of electrophoresis in polyacrylamide gels is used, their molecular weight is 93,000.
Flagellin molecules are characterized by a high content of serine, threonine, aspartic acid, glycine, alanine, and leucine. In comparison with the flagellin molecules of other bacteria those of Rhodopseudomonas palustris contain extremely high values of serine, threonine and glycine while the proportion of glutamic acid and arginine is relatively low. The flagellin molecule is built up of 158 amino acids.
The flagellar filament and the flagellar hook differ in content of total protein and of serine. The flagellar hook probably contains two protein components: one kind of molecule constitutes the core of the hook; an other kind of flagellin molecule is present in the central core. The serine content of flagellin of the central core is 45% higher than that of flagellin of the core.
It is postulated that the high content of serine may be responsible for the stability of the flagellar hooks through the development of hydrogen bridges. It is also assumed that the high level of amino acids with OH-groups in the core flagellin causes the binding of the subunits of flagellar sheath.
Zusammenfassung
Das Molekulargewicht der Flagellin-Moleküle der Rhodopseudomonas palustris-Geißeln konnte durch Ultrazentrifugation zu MG=15500 bestimmt werden; die Gelelektrophorese lieferte den sechsfachen Wert (MG=93000).
Die Flagellin-Moleküle sind gekennzeichnet durch einen sehr hohen Gehalt an Serin, Threonin, Asparaginsäure, Glycin, Alanin und Leucin. Verglichen mit Flagellin-Molekülen anderer Bakterien ist der molare Gehalt des Rhodopseudomonas palustris-Flagellins an Serin, Threonin und Glycin ungewöhnlich hoch, der Gehalt an Glutaminsäure und Arginin relativ niedrig. Das Flagellin-Molekül ist aus 158 Aminosäuren aufgebaut.
Geißelfilament und Geißelhaken unterscheiden sich durch ihren Protein- und Serin-Gehalt. Der Geißelhaken enthält voraussichtlich zwei Proteinkomponenten: Flagellin-Moleküle, die das Geißelhaken-(und Geißelfilament-)„core” aufbauen, und Flagellin-Moleküle, die das „central core” des Geißelhakens bilden. Das „central core”-Flagellin weist einen 45% höheren Seringehalt als das „core”-Flagellin auf.
Es wird die Hypothese aufgestellt, daß der hohe Seringehalt der „central core”-Untereinheiten verantwortlich ist für die Stabilität des Geißelhakens durch Ausbildung von Wasserstoffbrücken. Ebenfalls wird vermutet, daß der sehr hohe Gehalt des Rhodopseudomonas palustris-„core”-Flagellins an OH-Gruppen tragenden Aminosäuren eine Bindung der Scheidenuntereinheiten bewirkt.
Similar content being viewed by others
Literatur
Abram, D., Mitchen, J. R., Koffler, H., Vatter, A. E.: Differentiation within the bacterial flagellum and isolation of the proximal hook. J. Bact. 101, 250–261 (1970).
Bharier, M. A., Rittenberg, S. C.: Properties of axial filaments from Treponema zuelzerae and their relation to motility. Bact. Proc. 1970, 16, G 6.
Davis, B. J.: Disc electrophoresis. Ann. N. Y. Acad. Sci. 121, 404–427 (1964).
Erlander, S. R., Koffler, H., Foster, J. F.: Physical properties of flagellin from Proteus vulgaris, a study involving the application of the Archibald sedimentation principle. Arch. Biochem. 90, 139–153 (1960).
Gibbons, I. R.: The structure and composition of cilia. In: K. B. Warren (ed.): Formation and fate of cell organelles. Symp. Intern. Soc. Cell Biol., vol. 6, pp. 99–113. New York-London: Academic Press 1967.
Kerridge, D., Horne, R. W., Glauert, A. M.: Structural components of flagella from Salmonella typhimurium. J. molec. Biol. 4, 227–238 (1962).
Kobayashi, T., Rinker, J. N., Koffler, H.: Purification and chemical properties of flagellin. Arch. Biochem. 84, 342–362 (1959).
Maizel, J. V.: Acrylamide-gel electropherograms by mechanical fractionation: radioactive Adenovirus proteins. Science 151, 988–990 (1966).
Martinez, R. J., Brown, D. M., Glazer, A. N.: The formation of bacterial flagella. III. Characterization of the subunits of the flagella of Bacillus subtilis and Spirillum serpens. J. molec. Biol. 28, 45–51 (1967).
Masaki, T., Takaiti, O.: Some properties of chicken α-actinin. J. Biochem. 66, 637–643 (1969).
McDonough, M. W.: Amino acid composition of antigenically distinct Salmonella flagellar proteins. J. molec. Biol. 12, 342–355 (1965).
Mirsky, R.: Properties of flagellin from Bacillus megaterium KM and its association with the cytoplasmic membrane. Arch. Biochem. 39, 97–103 (1970).
Mitchen, J. R., Koffler, H., Smith, R. W.: Nature of flagellar hooks. Bact. Proc. 1970, 22 G51.
Nauman, R. K., Holt, S. C., Cox, C. D.: Purification, ultrastructure, and composition of axial filament from Leptospira. J. Bact. 98, 264–280 (1969).
Ornstein, L.: Disc electrophoresis. I. Background and theory. Ann. N. Y. Acad. Sci. 121, 321–349 (1964).
Parish, C. R., Ada, G. L.: Cleavage of bacterial flagellin with cyanogen bromide. Chemical and physical properties of the protein fragments. Biochem. J. 113, 489–499 (1969).
Shapiro, A. L., Vinuela, E., Maizel, J. V.: Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem. biophys. Res. Commun. 28, 815–820 (1967).
Shelanski, M. L., Taylor, E. W.: Properties of the protein subunit of central-pair and outer-doublet microtubules of sea urchin flagella. J. Cell Biol. 38, 304–315 (1968).
Stephens, R. E., Linck, R. W.: A comparison of muscle actin ciliary microtubule protein in the mollusk Pecten irradians. J. molec. Biol. 40, 497–501 (1969).
Tauschel, H.-D.: Zur Struktur des Geißelapparates von Rhodopseudomonas palustris. Zbl. Bakt., I. Abt. Orig. 212, 468–470 (1969).
—: Der Geißelapparat von Rhodopseudomonas palustris. IV. Isolierung der Geißel und ihrer Komponenten. Arch. Mikrobiol. 74, 193–206 (1970).
— Drews, G.: Der Geißelapparat von Rhodopseudomonas palustris. III. Untersuchungen zur Feinstruktur der Geißel. Cytobiol. 2, 87–107 (1970).
Valentine, R. C., Horne, R. W.: An assessment of negative staining techniques for revealing ultrastructure. In: R. J. C. Harris (ed.): The interpretation of ultrastructure, pp. 263–278. New York-London: Academic Press Inc. 1962.
Weibull, C.: Some chemical and physico-chemical properties of the flagella of Proteus vulgaris. Biochim. biophys. Acta (Amst.) 2, 351–361 (1948).
Yphantis, D. A.: Equilibrium ultracentrifugation of dilute solutions. Biochemistry 3, 297–317 (1964).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Tauschel, H.D. Der Geißelapparat von Rhodopseudomonas palustris . Archiv. Mikrobiol. 76, 91–102 (1971). https://doi.org/10.1007/BF00411783
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00411783