Ma Dejian, Fowler Jason D, Suo Zucai
Department of Biochemistry, The Ohio State University, Zucai Suo, 880 Biological Sciences, 484 West 12th Ave., Columbus, OH 43210, USA.
Biomol NMR Assign. 2011 Oct;5(2):195-8. doi: 10.1007/s12104-011-9298-1. Epub 2011 Feb 20.
Sulfolobus solfataricus DNA polymerase IV (Dpo4), a prototype Y-family DNA polymerase, contains a unique little finger domain besides a catalytic core. Here, we report the chemical shift assignments for the backbone nitrogens, α and β carbons, and amide protons of the little finger domain of Dpo4. This work and our published backbone assignment for the catalytic core provide the basis for investigating the conformational dynamics of Dpo4 during catalysis using solution NMR spectroscopy.
嗜热栖热菌DNA聚合酶IV（Dpo4）是Y家族DNA聚合酶的一个原型，除了催化核心外，还包含一个独特的小拇指结构域。在此，我们报道了Dpo4小拇指结构域的主链氮原子、α和β碳原子以及酰胺质子的化学位移归属。这项工作以及我们已发表的催化核心的主链归属，为利用溶液核磁共振光谱研究Dpo4催化过程中的构象动力学提供了基础。
