Argos P
EMBO J. 1985 May;4(5):1351-5. doi: 10.1002/j.1460-2075.1985.tb03784.x.
The primary structures of the recognition subunit (hsdS) in type I restriction enzymes from three isolates of Escherichia coli were compared and aligned by use of amino acid physical properties. A repeating domain was found in each of the subunits suggesting a pseudo-dimeric structure. Secondary structure predictions delineated two helical regions in each domain which suggested that the recognition subunits may act in a fashion similar to that proposed for repressor and activator molecules; namely, interaction with double-stranded DNA through helices and in two successive major grooves on the same DNA side. One helical motif could provide the specific recognition site and the other, the restriction site.
利用氨基酸物理性质,对来自三株大肠杆菌的I型限制酶识别亚基(hsdS)的一级结构进行了比较和比对。在每个亚基中都发现了一个重复结构域,提示其具有假二聚体结构。二级结构预测在每个结构域中勾勒出两个螺旋区域,这表明识别亚基的作用方式可能与阻遏物和激活分子类似;即通过螺旋与双链DNA相互作用,并在同一DNA链的两个连续大沟中进行。一个螺旋基序可提供特异性识别位点,另一个则提供限制位点。