1. Purified HrpA ofPseudomonas syringaepv.tomatoDC3000 reassembles into pili
- Author
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Nisse Kalkkinen, Juhani Saarinen, Elina Roine, and Martin Romantschuk
- Subjects
0106 biological sciences ,Protein Denaturation ,Molecular Sequence Data ,Size-exclusion chromatography ,Biophysics ,Pseudomonas syringae ,Biology ,01 natural sciences ,Biochemistry ,Pilus ,Microbiology ,Protein filament ,03 medical and health sciences ,Bacterial Proteins ,Solanum lycopersicum ,Structural Biology ,Pseudomonas ,Genetics ,Extracellular ,Denaturation (biochemistry) ,Amino Acid Sequence ,Molecular Biology ,Plant Diseases ,030304 developmental biology ,0303 health sciences ,Plant-microbe interaction ,Cell Biology ,In vitro ,Molecular Weight ,HrpA ,Fimbriae, Bacterial ,Type III secretion ,biology.protein ,Hrp pili ,Flagellin ,Bacterial Outer Membrane Proteins ,010606 plant biology & botany - Abstract
Pseudomonas syringae pv. tomato DC3000 produces Hrp pili under inducing in vitro conditions. A preparation of partially purified extracellular filaments contains HrpA, flagellin and some minor contaminants. HrpA was separated from the major contaminant, the flagellin, by gel filtration to a fraction containing HrpA as well as its three N-terminally truncated forms. These were further separated by two steps of reversed phase chromatography. HrpA and its degradation products were each shown to reassemble into filament structures after denaturation and renaturation showing that HrpA alone is sufficient for formation of filament structures.
- Published
- 1997
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