Choli T, Henning P, Wittmann-Liebold B, Reinhardt R
Abteilung Wittmann, Max-Planck-Institut für Molekulare Genetik, Berlin, Germany.
Biochim Biophys Acta. 1988 Jul 13;950(2):193-203. doi: 10.1016/0167-4781(88)90011-5.
DNA-binding proteins have been extracted from the thermoacidophilic archaebacterium Sulfolobus solfataricus strain P1, grown at 86 degrees C and pH 4.5. These proteins, which may have a histone-like function, were isolated and purified under standard, non-denaturing conditions, and can be grouped into three molecular mass classes of 7, 8 and 10 kDa. We have purified to homogenity the main 7 kDa protein and determined its DNA-binding affinity by filter binding assays and electron microscopy. The Stokes radius of gyration indicates that the protein occurs as a monomer. The complete amino-acid sequence of this protein contains 14 lysine residues out of 63 amino acids and the calculated Mr is 7149. Five of the lysine residues are partially monomethylated to varying extents and the methylated residues are located exclusively in the N-terminal (positions 4 and 6) and the C-terminal (positions 60, 62 and 63) regions only. The protein is strongly homologous to the 7 kDa proteins of Sulfolobus acidocaldarius with the highest homology to protein 7d. Accordingly, the name of this protein from S. solfataricus was assigned as DNA-binding protein Sso7d.
已从嗜热嗜酸古细菌嗜热栖热菌P1菌株中提取出DNA结合蛋白，该菌株在86摄氏度和pH值4.5的条件下生长。这些可能具有类组蛋白功能的蛋白在标准非变性条件下被分离和纯化，可分为分子量分别为7、8和10 kDa的三个类别。我们已将主要的7 kDa蛋白纯化至同质，并通过滤膜结合试验和电子显微镜确定了其DNA结合亲和力。斯托克斯旋转半径表明该蛋白以单体形式存在。该蛋白的完整氨基酸序列在63个氨基酸中有14个赖氨酸残基，计算出的分子量为7149。其中五个赖氨酸残基有不同程度的部分单甲基化，且甲基化残基仅位于N端（第4和6位）和C端（第60、62和63位）区域。该蛋白与嗜酸栖热菌的7 kDa蛋白高度同源，与蛋白7d的同源性最高。因此，来自嗜热栖热菌的这种蛋白被命名为DNA结合蛋白Sso7d。
