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Curr Genet. 1998 Aug;34(2):112-9.

Characterization of a galactose-1-phosphate uridylyltransferase gene from the marine red alga Gracilaria gracilis.

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  • 1Institute for Marine Biosciences, National Research Council of Canada, 1411 Oxford Street, Halifax, NS, Canada B3H 3Z1 and Department of Biology, Dalhousie University, Halifax, NS, Canada B3H 4J1.


The metabolism of D-galactose is a major feature of red-algal physiology. We have cloned and sequenced a gene from the red alga Gracilaria gracilis that encodes a key enzyme of D-galactose metabolism, galactose-1-phosphate uridylyltransferase (GALT). This gene, designated GgGALT1, is apparently devoid of introns. A potential TATA box, four potential CAAT boxes, and a repeated sequence occur in the 5'-flanking region. The predicted 369-aa peptide shares significant sequence similarity with GALTs from other organisms (human, 47%; Saccharomyces cerevisiae, 49%; Solanum tuberosum, 49%). Southern-hybridization analysis reveals two related, but apparently not identical, GALT genes in the nuclear genome of G. gracilis. Sequence analysis indicates that the GgGALT1 enzyme lacks a rubredoxin "knuckle" motif, which in bacterial and fungal GALTs is involved in binding zinc. An open reading frame encoding a potential peptidyl tRNA hydrolase occurs 179 bp downstream from the GgGALT1 gene.

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