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Glyceraldehyde-3-phosphate dehydrogenase gene from Zymomonas mobilis: cloning sequencing and identification of promoter region.

机译:运动发酵单胞菌中的甘油醛-3-磷酸脱氢酶基因:启动子区域的克隆测序和鉴定。

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摘要

The gene encoding glyceraldehyde-3-phosphate dehydrogenase was isolated from a library of Zymomonas mobilis DNA fragments by complementing a deficient strain of Escherichia coli. It contained tandem promoters which were recognized by E. coli but appeared to function less efficiently than the enteric lac promoter in E. coli. The open reading frame for this gene encoded 337 amino acids with an aggregate molecular weight of 36,099 (including the N-terminal methionine). The primary amino acid sequence for this gene had considerable functional homology and amino acid identity with other eucaryotic and bacterial genes. Based on this comparison, the gap gene from Z. mobilis appeared to be most closely related to that of the thermophilic bacteria and to the chloroplast isozymes. Comparison of this gene with other glycolytic enzymes from Z. mobilis revealed a conserved pattern of codon bias and several common features of gene structure. A tentative transcriptional consensus sequence is proposed for Z. mobilis based on comparison of the five known promoters for three glycolytic enzymes.
机译:通过补充缺陷型大肠杆菌从运动发酵单胞菌DNA片段文库中分离出编码甘油醛-3-磷酸脱氢酶的基因。它含有被大肠杆菌识别的串联启动子,但似乎比大肠杆菌中的肠lac启动子效率低。该基因的开放阅读框编码了337个氨基酸,总分子量为36099(包括N端甲硫氨酸)。该基因的一级氨基酸序列与其他真核和细菌基因具有相当的功能同源性和氨基酸同一性。基于该比较,来自运动发酵单胞菌的缺口基因似乎与嗜热细菌的缺口基因和叶绿体同工酶最密切相关。将该基因与运动发酵单胞菌的其他糖酵解酶进行比较,发现密码子偏倚的保守模式和基因结构的几个共同特征。基于三种糖酵解酶的五个已知启动子的比较,提出了运动发酵单胞菌的暂定转录共有序列。

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