| Autor: |
Kos T; Medical Biological Laboratory TNO, Rijswijk, The Netherlands., Kuijvenhoven A, Hessing HG, Pouwels PH, van den Hondel CA |
| Jazyk: |
angličtina |
| Zdroj: |
Current genetics [Curr Genet] 1988 Feb; Vol. 13 (2), pp. 137-44. |
| DOI: |
10.1007/BF00365648 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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