HU-α binds to the putative double-stranded DNA mimic HI1450 from Haemophilus influenzae
HU-α binds to the putative double-stranded DNA mimic HI1450 from Haemophilus influenzae
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DOI：
10.1110/ps.041275705
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发表时间：
2005-06-01
期刊：
影响因子：
8
通讯作者：
Orban, J
中科院分区：
文献类型：
--
作者：
Parsons, LM;Liu, F;Orban, J
最近，来自流感嗜血杆菌的假设蛋白质HI 1450的溶液结构被解决，作为基于结构的理解功能的努力的一部分。HI 1450的许多带负电荷的残基的分布以及与尿嘧啶DNA糖基化酶抑制剂（Ugi）的弱结构和序列同源性表明HI 1450可能充当双链DNA（dsDNA）模拟物。我们在这里提出了支持的证据，并表明HI 1450与dsDNA结合蛋白HU-α相互作用。HI 1450与H.流感病毒的特征使用量热法和NMR光谱学来表征。HU-alpha与HI 1450结合的Kd为3.0 +/- 0.2 μ M，其亲和力与其与dsDNA的相互作用相似。化学位移扰动数据表明HI 1450的β 1链和邻近区域最直接地参与与HU-α的相互作用。这些结果表明HI 1450及其结构同源物Ugi使用其结构的相似部分来识别DNA结合蛋白。
Recently, the solution structure of the hypothetical protein HI1450 from Haemophilus influenzae was solved as part of a structure-based effort to understand function. The distribution of its many negatively charged residues and weak structure and sequence homology to uracil DNA glycosylase inhibitor (Ugi) suggested that HI1450 may act as a double-stranded DNA (dsDNA) mimic. We present supporting evidence here and show that HI1450 interacts with the dsDNA-binding protein HU-alpha. The interaction between HI1450 and HU-alpha from H. influenzae is characterized using calorimetry and NMR spectroscopy. HU-alpha binds to HI1450 with a K-d of 3.0 +/- 0.2 mu M, which is similar in affinity to its interaction with dsDNA. Chemical shift perturbation data indicate that the beta 1-strand of HI1450 and neighboring regions are most directly involved in interactions with HU-alpha. These results show that HI1450 and its structural homolog, Ugi, use similar parts of their structures to recognize DNA-binding proteins.