Differentiation-related proteins of the broad bean rust fungus Uromyces viciae-fabae, as revealed by high resolution two-dimensional polyacrylamide gel electrophoresis
| Autor: | Peter Jungblut, Holger B. Deising, Kurt Mendgen |
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| Jazyk: | angličtina |
| Rok vydání: | 1991 |
| Předmět: |
Two-dimensional
Appressorium biology Hypha fungi Rust (fungus) Germ tube food and beverages General Medicine Infection structure differentiation biology.organism_classification Biochemistry Microbiology Thigmo-differentiation Uromyces Protein metabolism Isoelectric point Haustorium ddc:570 Genetics Molecular Biology Polyacrylamide gel electrophoresis Rust fungi polyacrylamide gel electrophoresis |
| Popis: | On artificial polyethylene membranes providing a thigmotropic signal, uredospores of the broad bean rust fungus Uromyces viciae-fabae differentiated a series of infection structures which in nature are necessary to invade the host tissue through the stomata. Within 24 h germ tubes, appressoria, substomatal vesicles, infection hyphae and haustorial mother cells were developed successively. Alterations in protein metabolism during infection structure differentiation of this obligate plant pathogen were analyzed in the absence of the host plant by high resolution two-dimensional polyacrylamide gel electrophoresis (2-DE) and silver staining. The norm pattern representing the 2-DE protein patterns of the whole developmental sequence of infection structures of U. viciae-fabae showed 733 spots. During infection structure differentiation 55 proteins were newly formed, altered in quantity, or disappeared. Major alterations in the protein pattern occurred during uredospore germination and when infection hyphae were formed. Uredospore germination was characterized by a decrease of acidic proteins and an increase mainly of proteins with isoelectric points ranging from weakly acidic to basic. |
| Databáze: | OpenAIRE |
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