1H, 13C, and 15N NMR assignments of the Pyrococcus abyssi DNA polymerase II intein.

Protein splicing is a precise post-translational process mediated by inteins. Inteins are intervening proteins that cleave themselves from a precursor protein while joining the flanking sequences. Here we report the 15N, 13C, and 1H chemical shift assignments of the intein from DNA polymerase II of Pyrococcus abyssi (Pab PolII intein), which has been recombinantly overexpressed and isotopically labeled. The NMR assignments of Pab PolII intein are essential for solution structure determination and protein dynamics study.

蛋白质剪接是一个由内含肽介导的精确翻译后过程。内含肽是一种间隔蛋白，它在连接两侧序列的同时从前提蛋白上自我切割下来。在此我们报道了来自深海火球菌（Pyrococcus abyssi）DNA聚合酶II的内含肽（Pab PolII内含肽）的15N、13C和1H化学位移归属，该内含肽已被重组过表达并进行了同位素标记。Pab PolII内含肽的核磁共振归属对于溶液结构测定和蛋白质动力学研究至关重要。