Kohler J J, Schepartz A
Department of Chemistry, Yale University, New Haven, Connecticut 06520-8107, USA.
Biochemistry. 2001 Jan 9;40(1):130-42. doi: 10.1021/bi001881p.
The bZIP proteins Fos and Jun bind DNA rapidly and with high affinity, forming a heteromeric complex that mediates activated transcription. Here we use stopped-flow fluorescence resonance energy transfer (FRET) to study the kinetic pathway by which Fos.Jun. DNA complexes assemble. Though dimerization of Fos and Jun occurs rapidly in the absence of DNA, the rate of dimerization is enhanced in the presence of DNA. Global analysis of the kinetic data shows that the favored DNA binding pathway is one is which the two protein monomers bind DNA sequentially and assemble their dimerization interface while bound to DNA.
碱性亮氨酸拉链（bZIP）蛋白Fos和Jun能快速且高亲和力地结合DNA，形成一种异源二聚体复合物，介导激活转录。在此，我们使用停流荧光共振能量转移（FRET）来研究Fos-Jun-DNA复合物组装的动力学途径。尽管在没有DNA的情况下Fos和Jun的二聚化迅速发生，但在有DNA存在时二聚化速率会提高。对动力学数据的整体分析表明，有利的DNA结合途径是两个蛋白质单体依次结合DNA，并在与DNA结合时组装其二聚化界面。
