Matsui T, Griniuviené B, Goldberg E, Tsugita A, Tanaka N, Arisaka F
Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
J Bacteriol. 1997 Mar;179(6):1846-51. doi: 10.1128/jb.179.6.1846-1851.1997.
A molecular chaperone of bacteriophage T4, gp57A, which facilitates the formation of the long and short tail fibers, was isolated and characterized by peptide analysis, sedimentation equilibrium, and circular dichroism (CD). Sequence analysis confirmed the predicted sequence of 79 amino acids from the nucleotide sequence of the gene with the N-terminal methionine removed. The result led to the conclusion that the apparent smaller molecular weight of 6,000 from Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis than the expected molecular weight of 8,710 was due to its abnormal electrophoretic behavior instead of cleavage or processing of the gene product. Estimation of the secondary structure from far-UV CD indicated a 94% alpha-helix content, which was in accord with the prediction from the primary structure. A sedimentation equilibrium study, on the other hand, revealed that gp57A assumes a tetrameric subunit structure.
噬菌体T4的一种分子伴侣gp57A,它促进长、短尾丝的形成,通过肽分析、沉降平衡和圆二色性(CD)进行分离和表征。序列分析证实了从去除N端甲硫氨酸的基因核苷酸序列预测的79个氨基酸序列。结果得出结论,在Tricine-十二烷基硫酸钠-聚丙烯酰胺凝胶电泳中,表观分子量为6000,低于预期分子量8710,这是由于其异常的电泳行为,而非基因产物的切割或加工。远紫外CD对二级结构的估计表明,α-螺旋含量为94%,这与一级结构的预测一致。另一方面,沉降平衡研究表明,gp57A呈现四聚体亚基结构。