Primary structure of phage mu transposase: homology to mu repressor.
Primary structure of phage mu transposase: homology to mu repressor.
复制标题
噬菌体 mu 转座酶的一级结构：与 mu 阻遏蛋白同源。
DOI：
10.1073/pnas.82.22.7676
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发表时间：
1985
影响因子：
11.1
通讯作者：
Chaconas,G
中科院分区：
文献类型：
--
作者：
Harshey,RM;Getzoff,ED;Baldwin,DL;Miller,JL;Chaconas,G
噬菌体Mu转座酶是整合、复制-转座和Mu DNA切除所必需的。我们展示了转座酶的完整核苷酸和衍生的氨基酸序列，并分析了转座酶/DNA相互作用的意义。Mu转座酶的NH2端与Mu抑制因子和Mu样噬菌体D108转座酶的NH2端具有相当大的序列同源性。已知这三种蛋白质在DNA上共享结合位点。蛋白质序列和预测的NH2末端的二级结构相似性表明，这三种蛋白质具有与已知结构蛋白质相似的共同dna结合区。Mu A蛋白的内部序列也具有这些特征。我们预计这些区域将在转位过程中参与DNA识别。
The phage Mu transposase is essential for integration, replication-transposition, and excision of Mu DNA. We present the complete nucleotide and derived amino acid sequence of the transposase and analyze implications for transposase/DNA interaction. The NH2 terminus of the Mu transposase has considerable sequence homology with the Mu repressor and with the NH2 terminus of the transposase of the Mu-like phage D108. These three proteins are known to share binding sites on DNA. The protein sequence and predicted secondary structural similarities at the NH2 termini of the three proteins suggest a common DNA-binding region similar to the regions found in proteins of known structure. An internal sequence in the Mu A protein also shares these features. We anticipate that these regions will be involved in DNA recognition during transposition.