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KMID : 0578319970070040548
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Molecules and Cells
1997 Volume.7 No. 4 p.548 ~ p.552
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Molecular characterization of a Nonsuppressible Allel (prc4)of the Drosophila purple Gene
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Kim Nack-Sung
Kim Jae-Seob
Kim Hee-Ryung
Park Dong-Kook
Yim Jeong-Bin
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Abstract
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Purple gene encodes 6-pyruvoyl tetrahydropterin synthase (PTP synthase) in Drosophila. The enzyme PTP sythase catalyzed the conversion of dihydroneopterin triphosphate (H_(2)-NTP) to 6-pyruvoyl tetrahydropterin (PTP), an important intermediate for pterin compounds. The extreme purple mutant, pr^(C4), shows a very low activity of PTP sythase. The mutant purple gene has been cloned by screening with the subgenomic library of pr^(C4). The size and expression level of PTP sythase gene transcripts in pr^(C4) were almost the same as those of the wild type. The genomic DNA was also examined in the purple region by Southern blot analysis, but no change in restriction pttern could be detected. Compared with the wild type PTP sythase sequence, the mutant PTP sythase of pr^(C4) showed three missense mutations: the replacement of alanine 7 by serine (A7S), leucine 9 by phenylalanine (L9P), and aspartic acid 168 by glycine (D168G). Significance of these mutations was discussed in relation to the formation of the oligomeric structure of PTP sythase.
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