Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.1.16 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
Search for more literature for 2.4.1.16

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

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

Subunits

Subunits Comment Organism
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

Synonyms Comment Organism
Chs8
-
 Ustilago maydis
Mcs1
-
 Ustilago maydis

General Information

General Information Comment Organism
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