PROTEIN-INDUCED BENDING AND DNA CYCLIZATION
PROTEIN-INDUCED BENDING AND DNA CYCLIZATION
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DOI：
10.1073/pnas.89.14.6343
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发表时间：
1992-07-15
影响因子：
11.1
通讯作者：
CROTHERS, DM
中科院分区：
文献类型：
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作者：
KAHN, JD;CROTHERS, DM
我们已经应用T4连接酶介导的DNA环化动力学蛋白质诱导的DNA弯曲。静态弯曲的存在和方向可以从150- 160-碱基对微环环化的J因子推断，其包括与序列定向弯曲相对应的分解代谢物激活蛋白结合位点。我们证明了一个准热力学环化和蛋白质结合之间的联系，我们发现，适当的相DNA结合分解代谢物激活蛋白几乎等于200倍更紧密的圆形比线性分子。这些结果明确区分了DNA弯曲和各向同性的柔性位点，并可以解释不需要相互接触的蛋白质的合作结合。
We have applied T4 ligase-mediated DNA cyclization kinetics to protein-induced bending in DNA. The presence and direction of a static bend can be inferred from J factors for cyclization of 150- to 160-base-pair minicircles, which include a catabolite activator protein binding site phased against a sequence-directed bend. We demonstrate a quasi-thermodynamic linkage between cyclization and protein binding; we find that properly phased DNAs bind catabolite activator protein almost-equal-to 200-fold more tightly as circles than as linear molecules. The results unambiguously distinguish DNA bends from isotropically flexible sites and can explain cooperative binding by proteins that need not contact each other.