Maher J F, Nathans D
Department of Molecular Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Proc Natl Acad Sci U S A. 1996 Jun 25;93(13):6716-20. doi: 10.1073/pnas.93.13.6716.
HMG-I proteins are DNA-binding proteins thought to affect the formation and function of transcription complexes. Each protein contains three DNA-binding motifs, known as AT-hooks, that bind in the minor groove of AT tracts in DNA. Multiple AT-hooks within a polypeptide chain should contact multiple AT tracts, but the rules governing these interactions have not been defined. In this study, we demonstrate that high-affinity binding uses two or three appropriately spaced AT tracts as a single multivalent binding site. These principles have implications for binding to regulatory elements such as the interferon beta enhancer, TATA boxes, and serum response elements.
HMG-I蛋白是一种DNA结合蛋白，被认为会影响转录复合物的形成和功能。每种蛋白都包含三个DNA结合基序，即所谓的AT钩，它们结合在DNA中AT序列的小沟内。一条多肽链中的多个AT钩应该与多个AT序列接触，但这些相互作用的规则尚未明确。在本研究中，我们证明高亲和力结合使用两个或三个间隔适当的AT序列作为单个多价结合位点。这些原理对于与调控元件如干扰素β增强子、TATA盒和血清反应元件的结合具有重要意义。
