FGSC #4220

Mutant Type

Genus: N

reporting_genes: set-2;sit-3;arg-5;ota

species: Neurospora crassa

allele: GN328;GN235;no#;UM728

stock: 328/235(3-1)

glasgow:

mutagen:

Depositor: GWC

Link Group: --;--;IIR;IIIR

MT: A

Species No: 10

gene_back:

oppmt: 0

trans:

ref1: Charlang and Williams 1983 Neurospora Newsl 30:6-7, https://doi.org/10.4148/1941-4765.1617

ref2:

site:

country:

ksudc_link: https://digital.lib.k-state.edu/item/neurospora-crassa/fgsc-4220

ksudc_link_html: https://digital.lib.k-state.edu/item/neurospora-crassa/fgsc-4220 ↗

Genes

Locus	Cultural Requirements	Link Group	Type
arg-5	Uses ornithine, citrulline or arginine.	IIR	B
ota	IIIR. Between ad-4 (15%) and tyr-1 (14%) (241). Linked to pro-4 (4%) (D.J. West, cited in Neurospora Newsl. 16:19-22, 1970). Ornithine-delta-transaminase deficient (241) (Fig. 10). Conidiates somewhat less than does the wild type (S. Brody, personal communication). Selected by ability to use exogenous ornithine as a precursor for arginine in an arg-5 arg-12s double mutant. Catabolism of ornithine (to glutamic-gamma-semialdehyde) is blocked, resulting in ornithine concentrations high enough to compensate for the low activity of the ornithine carbamyl transferase in the arg-12s mutant. The ota single mutant is prototrophic but prevents the efficient use of ornithine or arginine as the sole nitrogen source (241). Used to study flux through the arginine biosynthetic pathway (401). Used to study the utilization of endogenous versus exogenous ornithine (234). Sideramine production is completely blocked in absence of ornithine in the ota;arg-5;aga triple mutant, which is used to study iron transport (1146, 1147).	IIIR	B
sit-3	Unmapped. Defective uptake of exogenous ferricrocin and coprogen. Several mutations are known that represent at least three loci. Selected in triple mutant aga;arg-5;ota (G.W. Charlang and N.P. Williams, personal communication), which is blocked in the known pathways to ornithine (240) and thus depleted of siderophores. (1147, G. W. Charlang and N. P. Williams, personal communications). Transport of siderophores is severly reduced. Binding is normal.		B
set-2			B