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Der Geißelapparat von Rhodopseudomonas palustris

VI. Charakterisierung des Flagellins

The flagellar apparatus of Rhodopseudomonas palustris

VI. Characterization of flagellin

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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.

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Tauschel, H.D. Der Geißelapparat von Rhodopseudomonas palustris . Archiv. Mikrobiol. 76, 91–102 (1971). https://doi.org/10.1007/BF00411783

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  • DOI: https://doi.org/10.1007/BF00411783

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