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DNA sequence of the D-serine deaminase activator gene dsdC.

机译:D-丝氨酸脱氨酶激活基因dsdC的DNA序列。

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We have determined the DNA sequence of dsdC, the gene that encodes the D-serine deaminase activator protein of Escherichia coli K-12. The sequence contains a single open reading frame that terminates in a UGA codon. One the basis of the size of the protein, 33 kilodaltons, and the amino acid sequence encoded by the open reading frame, we identified a likely translation initiation codon 731 base pairs upstream of the translation initiation codon for the divergently transcribed D-serine deaminase gene. There is a broad range of codon usage, not surprising in view of the weak expression of the gene. The N-terminal two-thirds of the activator is arginine-lysine rich and quite polar; the remainder is more neutral. The segment of the protein that seems most likely to have potential to form the helix-turn-helix structure characteristic of DNA-regulatory proteins is located near the end of the polar region. The protein contains a region with significant homology to lambda attB.
机译:我们已经确定了dsdC的DNA序列,该基因编码大肠杆菌K-12的D-丝氨酸脱氨酶激活蛋白。该序列包含一个终止于UGA密码子的开放阅读框。根据蛋白质大小(33千道尔顿)和开放阅读框编码的氨基酸序列的基础,我们确定了转录转录的D-丝氨酸脱氨酶基因翻译起始密码子上游可能存在的翻译起始密码子731个碱基对。 。密码子的使用范围很广,鉴于基因的弱表达,这不足为奇。活化剂的N端三分之二是富含精氨酸和赖氨酸的,并且极性很大。其余的则比较中立。似乎最有可能形成DNA调控蛋白特有的螺旋-转-螺旋结构特征的蛋白质片段位于极性区域的末端附近。该蛋白质包含与λattB具有显着同源性的区域。

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