Mistiniene Edita, Luksa Virginijus, Sereikaite Jolanta, Naktinis Vytautas
Institute of Biotechnology, V. Graiciūno 8, Vilnius 2028, Lithuania.
Bioconjug Chem. 2003 Nov-Dec;14(6):1243-52. doi: 10.1021/bc0341066.
Proteins UK114 and p14.5 are both members of the putative family of small proteins YER057c/YIL051c/YjgF. The biological role of these proteins is not understood very well, and in addition, their oligomeric structure in solution remains controversial. We therefore investigated the oligomeric structure of UK114 and p14.5 using a number of methods. Both proteins have exhibited a homotrimeric structure in solution. Indeed the trimeric structure of the two proteins appeared to be so similar that when protein subunits derived from different species were mixed, stable heterotrimeric complexes (monomer ratio of 1:2 and 2:1 of UK114 and p14.5, respectively) could be formed in vitro. Furthermore, the trimeric structure of both UK114 and p14.5 proved essential for the stoichiometric hydrophobic ligand, such as fatty acid binding activity of the two proteins.
蛋白质UK114和p14.5都是假定的小蛋白质YER057c/YIL051c/YjgF家族的成员。这些蛋白质的生物学作用尚未被很好地理解,此外,它们在溶液中的寡聚结构仍存在争议。因此,我们使用多种方法研究了UK114和p14.5的寡聚结构。两种蛋白质在溶液中均呈现同三聚体结构。实际上,这两种蛋白质的三聚体结构看起来非常相似,以至于当来自不同物种的蛋白质亚基混合时,体外可以形成稳定的异三聚体复合物(UK114和p14.5的单体比例分别为1:2和2:1)。此外,UK114和p14.5的三聚体结构对于化学计量疏水配体(如两种蛋白质的脂肪酸结合活性)被证明是必不可少的。