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化学合成的触角足同源结构域与特定的DNA序列结合。

A chemically synthesized Antennapedia homeo domain binds to a specific DNA sequence.

作者信息

Mihara H, Kaiser E T

机构信息

Laboratory of Bioorganic Chemistry and Biochemistry, Rockefeller University, New York, NY 10021.

出版信息

Science. 1988 Nov 11;242(4880):925-7. doi: 10.1126/science.2903553.

Abstract

A peptide 60 residues in length that corresponds to the homeo domain of Antennapedia (Antp), a protein governing development in Drosophila, was synthesized by segment condensation with protected peptide segments prepared on an oxime resin. A footprinting assay showed that the homeo domain binds specifically to a TAA repeat DNA sequence in the Antp gene. Thus the Antp homeo domain has a sequence-specific DNA binding property. The circular dichroism spectra of the homeo domain peptide showed the presence of a significant amount of alpha-helical structure in aqueous solution and in 50 percent trifluoroethanol. The alpha helicity measured in water appears to depend on the peptide concentration, which suggests that the peptide aggregates. These results support the hypothesis that the homeo domain binds to DNA through a helix-turn-helix motif.

摘要

合成了一段长度为60个残基的肽段,它对应于触角足蛋白(Antp)的同源结构域,触角足蛋白是一种控制果蝇发育的蛋白质,该肽段通过与在肟树脂上制备的受保护肽段进行片段缩合反应合成。足迹分析表明,该同源结构域与Antp基因中的一个TAA重复DNA序列特异性结合。因此,Antp同源结构域具有序列特异性DNA结合特性。同源结构域肽段的圆二色光谱表明,在水溶液和50%三氟乙醇中存在大量的α-螺旋结构。在水中测得的α-螺旋度似乎取决于肽段浓度,这表明肽段会聚集。这些结果支持了同源结构域通过螺旋-转角-螺旋基序与DNA结合的假说。

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