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Literature summary extracted from

  • Treitschke, S.; Doehlemann, G.; Schuster, M.; Steinberg, G.
    The myosin motor domain of fungal chitin synthase V is dispensable for vesicle motility but required for virulence of the maize pathogen Ustilago maydis (2010), Plant Cell, 22, 2476-2494.
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.16 Ustilago maydis Q4P9K9 isoform Mcs1, class V chitin synthase
-

Subunits

EC Number Subunits Comment Organism
2.4.1.16 More protein consists of a myosin motor domain fused to a membrane-spanning chitin synthase region. Both domains are required for fungal virulence. Fungi carrying mutations in the chitin synthase domain are rapidly recognized and killed by the plant, whereas fungi carrying a deletion of the motor domain show alterations in cell wall composition but can invade host tissue and cause a moderate plant response Ustilago maydis

Synonyms

EC Number Synonyms Comment Organism
2.4.1.16 Chs8
-
 Ustilago maydis
2.4.1.16 Mcs1
-
 Ustilago maydis

General Information

EC Number General Information Comment Organism
2.4.1.16 physiological function isoform Mcs1 consists of a myosin motor domain fused to a membrane-spanning chitin synthase region. Both domains are required for fungal virulence. Fungi carrying mutations in the chitin synthase domain are rapidly recognized and killed by the plant, whereas fungi carrying a deletion of the motor domain show alterations in cell wall composition but can invade host tissue and cause a moderate plant response. Mcs1-bound vesicles exhibit long-range movement for up to 20 mm at a velocity of ;1.75 microm/s. Apical Mcs1 localization depends on F-actin and the motor domain, whereas Mcs1 motility requires microtubules and persists when the Mcs1 motor domain is deleted Ustilago maydis