Purification, characterization and reassembly of the bacteriophage T4D tail sheath protein P18.
Purification, characterization and reassembly of the bacteriophage T4D tail sheath protein P18.
复制标题
噬菌体 T4D 尾鞘蛋白 P18 的纯化、表征和重组。
DOI：
10.1016/0022-2836(79)90128-1
复制
发表时间：
1979
影响因子：
5.6
通讯作者：
J. Engel
中科院分区：
文献类型：
--
作者：
J. Tschopp;F. Arisaka;R. Driel;J. Engel
P18是T4尾鞘的唯一成分，已从低离子强度下解离的完整尾鞘中以单体活性形式分离出来。沉淀法测得P18的相对分子质量为65,000，十二烷基硫酸钠/凝胶电泳法测得P18的相对分子质量为73,000。结合扩散常数(D20，w=5.5×10−7cm2s−1)和沉积常数(S020，w=4·2 S)，得到67,000。圆二色谱表明，P18在单体状态和扩展鞘构象中的结构非常相似，如果存在核-基板复合体，纯化的P18可以重组成扩展鞘，形成正常长度的尾巴。在没有核心-基板的情况下，形成类似于多鞘的结构。
P18, the sole component of T4 tail sheath, has been isolated in a monomeric active form from extended sheaths of intact tails which were dissociated at low ionic strength. The molecular weight of P18 is determined to be 65,000 from sedimentation equilibrium and 73,000 from sodium dodecyl sulphate/gel electrophoresis. Combining the diffusion constant (D20,w= 5·5× 10−7cm2s−1)and the sedimentation constant (s020,w= 4·2 S) a value of 67,000 is obtained. The circular dichroism spectra reveal a striking similarity of the structure of P18 in the monomeric state and in the extended sheath conformation.The purified P18 is found to reassemble into extended sheaths if the core-baseplate complex is present, forming normal length tails. Structures similar to polysheath are formed in the absence of core-baseplates.