FGSC #4546

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Reporting Genes: trp-3 aro-9;qa-2

Species: crassa

Allele: td24 Y325M6 M246

Alternate Strain Number: 9330

Depositor: DDP

Linkage Group: IIR R;VII

Mating Type: a

Species Number: 10

Deposit Sheet ↗

Genes

Locus	Cultural Requirements	Link Group	Type
aro-9	Requires shikimic acid or a mixture of the four aromatic amino acids when combined with qa-1. Single mutant grows on minimal media.	IIR	B
qa-2	VII. In the qa cluster between qa-4 and met-7 (0.02%) (146). (884) Lacks catabolic dehydroquinase (148, 517, 884). Unable to use quinate or shikimate as the sole carbon source in the presence of aro-9, which results in the absence of biosynthetic dehydroquinase (885) (Fig. 21). aro-9;qa-2+ strains grow on minimal medium without supplement. qa-2 is conveniently scored as an aro auxotroph when aro-9 is present. qa-2+ cloned in pBR322 (pVK57) is expressed constitutively from its own promoter in E. coli(23, 388, 451); has been returned to Neurospora chromosomal sites by transformation (150). Allele M246 is stable (150).	VII	B
trp-3	IIR. Right of fl (2 to 6%). Left of rip-1 (9%) and un-5(10%) (816, PB). (1166). Uses tryptophan (685); strains carrying some alleles also use indole (4). Structural gene for tryptophan synthetase (1167), called tryptophan desmolase in early literature. Tryptophan synthetase catalyzes three reactions: indoleglycerol-phosphate -> tryptophan, indole tryptophan, and indoleglycerol-phosphate <-> indole (Fig. 11). In Neurospora, all three reactions are catalyzed by a single protein, which is specified by a single gene (645, 1167). Mutants lack indoleglycerol-phosphate -> tryptophan activity but differ with respect to the other activities; e.g., strains carrying trp-3 allele (td141 are blocked in indoleglycerol-phosphate utilization but can use indole; trp-3 (td100) can synthesize indole but not convert it to tryptophan; trp-3 (td140) lacks all three activities. (See references 582 and 1049 for citations and characteristics of other mutants.) Used extensively for studies of gene structure in relation to enzymatic activity (257, 582 and references therein, 1167). The active enzyme is a homooligomer (645) thought to have two domains (644 and references therein). Biochemical studies of complementation between alleles: in vivo (582, 583) and in vitro (1048 and references therein). Complementation maps (4, 5, 9 and references therein, 582). Fine-structure maps (5, 540, 582, 1049). Reviewed as example of gene fusion (218). trp-3 mutant C83 provided the first proved example in Neurospora of gene-controlled loss of enzyme activity (685); trp-3 mutant S1952 provided the first example of allele-specific suppression restoring functional wild-type-like enzyme (1166). Allele td140 is supersuppressible (954, 955). Certain classes of trp-3mutants are osmotic remediable (583). Called td and tryp-3.	IIR	B