甲酰化起始tRNA与大肠杆菌RNA聚合酶的特异性结合。
Specific binding of formylated initiator-tRNA to Escherichia coli RNA polymerase.
作者信息
Pongs O, Ulbrich N
出版信息
Proc Natl Acad Sci U S A. 1976 Sep;73(9):3064-7. doi: 10.1073/pnas.73.9.3064.
Abstract
E. coli fMet-tRNAfMEet and E. coli RNA plymerase (RNA nucleotidyltransferase; EC 2.7.7.6; nucleoside-triphosphate:RNA nucleotidyltransferase) form a 1:1 complex with an apparent association constant of 9.0 X 10(6)M-1 at 37 degrees. The affinity of polymerase to tRNA depends on the tRNA as well as the formyl methionine moiety. Core polymerase has a greatly reduced affinity for initiator tRNA. Optimal binding conditions are similar to those that are also optimal for binding initiator tRNA to ribosomes. Binding of initiator tRNA to polymerase stimulates the transcription of lambda plac DNA, as determined in a crude cell-free system for beta-galactosidase (EC 3.2.1.23; beta-D-galactoside galactohydrolase) synthesis as well as in a highly purified transcription system.
摘要
大肠杆菌甲酰甲硫氨酰 - tRNAfMet与大肠杆菌RNA聚合酶（RNA核苷酸转移酶；EC 2.7.7.6；核苷三磷酸：RNA核苷酸转移酶）在37℃下形成1:1复合物，其表观缔合常数为9.0×10⁶M⁻¹。聚合酶对tRNA的亲和力取决于tRNA以及甲酰甲硫氨酸部分。核心聚合酶对起始tRNA的亲和力大大降低。最佳结合条件与起始tRNA与核糖体结合的最佳条件相似。如在用于β - 半乳糖苷酶（EC 3.2.1.23；β - D - 半乳糖苷半乳糖水解酶）合成的粗无细胞系统以及高度纯化的转录系统中所测定的，起始tRNA与聚合酶的结合刺激了λplac DNA的转录。
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