Nucleotide sequence of the Aspergillus niger trpC gene: structural relationship with analogous genes of other organisms.
The nucleotide sequence of the Aspergillus niger tryptophan C (trpC) gene was determined. Northern hybridization and S1-mapping experiments showed the presence of a 2.6 kb trpC poly(A)+ RNA with two very short (5 and 6 nucleotides) noncoding 5'-regions. Comparison of the predicted amino acid sequence with that of trp gene proteins of pro- and eukaryotic organisms revealed three functional domains (G, C, F) in the A. niger TrpC protein which catalyse the glutamine amidotransferase reaction (GAT), the indole-3-glycerol phosphate synthase reaction (IGPS) and the N-(5'-phosphoribosyl) anthranilate isomerase reaction (PRAI), respectively. These domains are highly conserved and bordered by short areas showing less homology. Within the F domain of the trpC gene in A. niger, A. nidulans and Neurospora crassa, a region encoding 30 amino acids was found which is absent in the analogous genes of Saccharomyces cerevisiae and prokaryotic organisms. This region has features of a mutated in-phase intron.
Kos
T
T
Medical Biological Laboratory TNO, Rijswijk, The Netherlands.
Kuijvenhoven
A
A
Hessing
H G
HG
Pouwels
P H
PH
van den Hondel
C A
CA
D000595:Amino Acid Sequence; D001234:Aspergillus niger / Q000235:genetics*; D001483:Base Sequence; D004262:DNA Restriction Enzymes; D005796:Genes; D005800:Genes, Fungal; D005809:Genes, Regulator; D008969:Molecular Sequence Data; D011401:Promoter Regions, Genetic; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity; D014364:Tryptophan / Q000096:biosynthesis*
D014364:Tryptophan; D004262:DNA Restriction Enzymes