FGSC #7924

Mutant Type

Genus: N

reporting_genes: pmb;aga

species: Neurospora crassa

allele: DF101;UM906

stock: IC2842-4A

glasgow:

mutagen: UV

Depositor: RHD

Link Group: IVR;VIIR

MT: A

Species No: 10

gene_back:

oppmt: 7925

trans:

ref1: Davis et al. 1994. Genetics 138:649-655, https://doi.org/10.1093/genetics/138.3.649

ref2:

site:

country:

ksudc_link: https://digital.lib.k-state.edu/item/neurospora-crassa/fgsc-7924

ksudc_link_html: https://digital.lib.k-state.edu/item/neurospora-crassa/fgsc-7924 ↗

Genes

Locus	Cultural Requirements	Link Group	Type
pmb	IVR. Right of uvs-2 (8%) (S. Ogilvie-Villa, cited in reference 248; R. Sadler and S. Ogilvie-Villa, personal communication). Defective in basic L-amino acid transport (system III as defined in reference 778); reduced uptake of L-arginine, L-lysine, and L-histidine (778, 1152, 1076). Used extensively for transport studies; see reference 1150. Altered surface glycoprotein (1038). pmb mutants selected as resistant to L-canavanine (889, 1152). Allelic with bat (R. Sadler and S. Ogilvie-Villa, personal communication), which was selected in arg-12s;pyr-3 (CPS- ACT+) by ability to grow on minimal medium plus arginine, when the parental double mutant was not able to grow because of arginine uptake and feedback onto the arginine-specific carbamyl phosphate synthase (1074). Possibly allelic with basa, which was selected by the inability of the mutant his-3 to grow on histidine plus methionine (628). Probably allelic with bm-1 (linked to pyr-2, 24%), which was selected by canavanine resistance (913). Probably allelic with argR (565, 566), q.v. Called Cr-10, Pm-B, pm b, UM-535, and can-37. See Transport.	IVR	B
aga	VIIR. Between wc-1 (2%) and arg-10 (24 to 27%) (240, 697). Presumed structural gene for arginase (240, 697) (see Fig. 10). Unable to form ornithine from arginine; arginine is thus unable to satisfy the proline requirement of pro-3 in a pro-3 aga double mutant. Prototrophic single mutants develop polyamine requirement in the presence of arginine. This is due to feedback inhibition of ornithine biosynthesis by arginine, combined with a catabolic block in ornithine formation from arginine (240). Siderophore production is severely reduced in the absence of ornithine in the triple mutant aga arg-5 ota, which has been used to study iron transport (1146, 1147) and to obtain mutants defective in siderophore uptake (G.W. Charlang and N.P. Williams, personal communication); see sit.	VIIR	B