COMPARISON OF THE CIS-ACTING CONTROL REGIONS OF 2 COORDINATELY CONTROLLED GENES INVOLVED IN ETHANOL UTILIZATION IN ASPERGILLUS-NIDULANS
COMPARISON OF THE CIS-ACTING CONTROL REGIONS OF 2 COORDINATELY CONTROLLED GENES INVOLVED IN ETHANOL UTILIZATION IN ASPERGILLUS-NIDULANS
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DOI：
10.1016/0378-1119(87)90309-x
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发表时间：
1987-01-01
期刊：
影响因子：
3.5
通讯作者：
SEALYLEWIS, HM
中科院分区：
文献类型：
--
作者：
GWYNNE, DI;BUXTON, FP;SEALYLEWIS, HM
构巢曲霉的alcA和aldA基因以完全相同的方式调节，受到alcR基因产物的正控制。我们报道了alcA基因及其5“非编码区的完整核苷酸序列，参与alcA表达调节的区域的初步定位，以及该区域与aldA的5”非编码区的详细比较（Pickett等人，1987年）。基因的5“侧翼区含有6个相似的序列元件。这些元件中的三个位于信使RNA起始点的上游，并且一个与在负责酵母ADH 2基因的乙醇诱导的区域中发现的序列元件相关（Beier等人，1985年）。其他同源元件位于信使RNA前导序列内，可能与信使RNA起始点的选择有关。醇脱氢酶I的氨基酸序列（348个残基）与其他生物体中的类似序列具有显著的同源性。基因alcA含有内含子，其在大小和结构上与其他真菌内含子相似。本文讨论了A.特别是关于具有NAD结合结构域的酶中内含子位置的保守性和进化组装。
The alcA and aldA genes of Aspergillus nidulans are regulated in exactly the same manner, being subject to positive control by the product of the alcR gene. We report the complete nucleotide sequence of the alcA gene and its 5'' non-coding region, preliminary localization of the region involved in the regulation of alcA expression, and a detailed comparison of this region to the 5'' non-coding region of aldA (Pickett et al., 1987). The 5'' flanking regions of the genes contain six similar sequence elements. Three of these elements are located upstream from the messenger RNA start points and one is related to a sequence element found in the region responsible for ethanol induction of the yeast ADH2 gene (Beier et al., 1985). The other homologous elements are located within the messenger RNA leader and may be associated with selection of messenger RNA start points. The amino acid sequence of alcohol dehydrogenase I (348 residues) shows a significant level of homology with analogous sequences in other organisms. Gene alcA contains introns which are similar in size and structure to other fungal introns. We discuss the positions of the introns in alcA of A. nidulans with particular reference to the conservation of intron position in and the evolutionary assembly of enzymes which possess NAD-binding domains.