CLOSELY RELATED TRANSCRIPTS ENCODED BY THE NEUROGENIC GENE-COMPLEX ENHANCER OF SPLIT OF DROSOPHILA-MELANOGASTER
CLOSELY RELATED TRANSCRIPTS ENCODED BY THE NEUROGENIC GENE-COMPLEX ENHANCER OF SPLIT OF DROSOPHILA-MELANOGASTER
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DOI：
10.1002/j.1460-2075.1989.tb03365.x
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发表时间：
1989-01-01
期刊：
影响因子：
11.4
通讯作者：
CAMPOSORTEGA, JA
中科院分区：
文献类型：
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作者：
KLAMBT, C;KNUST, E;CAMPOSORTEGA, JA
遗传学证据表明，E（spl），果蝇的神经基因座之一，是一个基因复合体，包括一个尚未完全建立的转录单位的数量。为了将各种转录单位与E（spl）功能相关联，用编码来自突变体E（spl）D的转录单位m8的基因组DNA转化野生型果蝇，已知突变体E（spl）D在携带该突变体等位基因的胚胎中发生改变。转化体显示出与E（spl）D本身相同的spl表型的显性增强。由于m8与m4、m5和m7具有几乎相同的表达模式，我们确定了这些fur转录物的序列。m5、m7和m8的蛋白质产物具有广泛的序列同源性。所有这三个编码一个序列类似于一个保守的结构域的脊椎动物myc基因家族的代表，这也是目前在推导的蛋白质序列的果蝇achaete-scute基因复合物。在E（spl）D突变的m8转录单位的序列分析显示几个DNA损伤。病变之一是转录起始位点上游区域的缺失。另一个损伤是编码区的缺失，其导致更短的蛋白质，此外，其羧基末端与野生型蛋白质的不同之处在于存在9个氨基酸。
Genetic evidence suggests that E(spl), one of the neurogenic loci of Drosophila, is a gene complex comprising an as yet incompletely established number of transcription units. In order to correlate the various transcription units with E(spl) functions, wild-type flies were transformed with genomic DNA encoding the transcription unit m8 from the mutant E(spl)D, which was known to be altered in embryos carrying this mutant allele. Transformants show the same dominant enhancement of the spl phenotype as E(spl)D itself. Since m8 has a virtually identical pattern of expression as m4, m5 and m7, we have determined the sequence of these fur transcripts. The deduced protein products of m5, m7 and m8 exhibit extensive sequence homology with each other. All three encode a sequence similar to one of the conserved domains of representatives of the vertebrate myc gene family which is also present in the deduced protein sequences of the Drosophila achaete-scute gene complex. Sequence analysis of the m8 transcription unit in the E(spl)D mutation revealed several DNA lesions. One of the lesions is a deletion in the region upstream of the transcription start site. Another lesion is a deletion in the coding region that leads to a shorter protein which, in addition, differs in its carboxy-terminal end from the wild-type protein by the presence of nine amino acids.