Luo Shi-Zhong, Li Yan-Mei, Qiang Wei, Zhao Yu-Fen, Abe Hiroshi, Nemoto Tadashi, Qin Xu-Rong, Nakanishi Hiroshi
The Key Laboratory for Bioorganic Phosphorus Chemistry, Ministry of Education, Department of Chemistry, Tsinghua University, Beijing, China.
J Am Soc Mass Spectrom. 2004 Jan;15(1):28-31. doi: 10.1016/j.jasms.2003.08.008.
Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry was used to obtain spectra of peptide-DNA complexes formed by basic domain (BD15) of c-Fos protein and DNA AP-1 site (5'-TGAGTCA-3'). The noncovalent interaction between single stranded DNA and BD15 was observed and confirmed to be an ionic one between the negatively charged sugar-phosphate backbone of DNA and positively charged side chains of Arg- and lys-rich peptides as demonstrated by Vertes and coworkers and Woods and coworkers. But the specific noncovalent interaction between DNA AP-1 site and the dimer of BD15 was firstly detected in this paper. Various different sequence DNAs were studied and it was found that this interaction is a sequence-specific one, and AP-1 site was essential for this interaction. This specific interaction depends on the matrix. It was only observed in the ATT matrix and not in the other two matrixes (CHCA and DHBA).
基质辅助激光解吸/电离（MALDI）质谱用于获取由c-Fos蛋白的碱性结构域（BD15）与DNA AP-1位点（5'-TGAGTCA-3'）形成的肽-DNA复合物的光谱。如Vertes及其同事以及Woods及其同事所证明的，观察到单链DNA与BD15之间的非共价相互作用，并证实其为DNA带负电荷的糖磷酸主链与富含精氨酸和赖氨酸的肽的带正电荷侧链之间的离子相互作用。但本文首次检测到DNA AP-1位点与BD15二聚体之间的特异性非共价相互作用。研究了各种不同序列的DNA，发现这种相互作用是序列特异性的，并且AP-1位点对于这种相互作用至关重要。这种特异性相互作用取决于基质。仅在ATT基质中观察到，而在其他两种基质（CHCA和DHBA）中未观察到。
