Potter H, Dressler D
Proc Natl Acad Sci U S A. 1980 May;77(5):2390-4. doi: 10.1073/pnas.77.5.2390.
This paper describes an enzyme from Escherichia coli, and its purification to apparent homogeneity. The protein, which we call "DNA synaptase" and which may be representative of a class of enzymes, fuses double-stranded DNA molecules at a region of homology. In addition, the purified enzyme is able to catalyze the association of single-stranded DNA with homologous duplex DNA. The genome fusion reaction catalyzed by the purified enzyme occurs in the presence of Mg2+, spermidine, and 2-mercaptoethanol and does not require a high-energy cofactor. By bringing two genomes together at a region of homology, DNA synaptase has a property expected for an enzyme that participates in an early step in genetic recombination. However, the synaptase can be recovered from Rec A- cells, and thus it is not yet possible to determine whether this enzyme plays a role in physiological recombination or in another cellular process that involves genome fusion, such as the recombinational repair of damaged DNA.
本文描述了一种来自大肠杆菌的酶及其纯化至表观均一性的过程。这种蛋白质,我们称之为“DNA 突触酶”,它可能代表了一类酶,能在同源区域融合双链 DNA 分子。此外,纯化后的酶能够催化单链 DNA 与同源双链 DNA 的结合。纯化后的酶所催化的基因组融合反应在 Mg2+、亚精胺和 2-巯基乙醇存在的情况下发生,并且不需要高能辅助因子。通过在同源区域将两个基因组聚集在一起,DNA 突触酶具有参与基因重组早期步骤的酶所预期的特性。然而,突触酶可以从 Rec A-细胞中回收,因此尚无法确定这种酶是否在生理重组或涉及基因组融合的其他细胞过程(如受损 DNA 的重组修复)中发挥作用。