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

被引：0
|
作者：
A. O. Lluisma
M. A. Ragan
机构：
[1] Institute for Marine Biosciences,
[2] National Research Council of Canada,undefined
[3] 1411 Oxford Street,undefined
[4] Halifax,undefined
[5] NS,undefined
[6] Canada B3H 3Z1 and Department of Biology,undefined
[7] Dalhousie University,undefined
[8] Halifax,undefined
[9] NS,undefined
[10] Canada B3H 4J1,undefined
[11] Institute for Marine Biosciences,undefined
[12] National Research Council of Canada,undefined
[13] 1411 Oxford Street,undefined
[14] Halifax,undefined
[15] NS,undefined
[16] Canada B3H 3Z1 and Canadian Institute for Advanced Research in Evolutionary Biology e-mail: mark.ragan@nrc.ca Tel.: +1-902-426 1674 Fax: +1-902-426 9413,undefined
来源：
Current Genetics | 1998年 / 34卷
关键词：
Key wordsGracilaria gracilis; Rhodophyceae; Galactose metabolism; Nuclear gene; Uridylyltransferase;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
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.
引用
收藏
页码：112 / 119
页数：7
相关论文
共 50 条
12345