Structure and flexibility adaptation in nonspecific and specific protein-DNA complexes (Science, 2004, 305:386-389)

報告日期: 2006/04/11
報告時間: 16:00/16:50
報告學生: 張家豪
講評老師: 蔡少正


Structure and Flexibility Adaptation in Nonspecific and Specific Protein-DNA Complexes


16 JULY 2004 VOL 305 SCIENCE

Speaker: 張家豪                  Commentator: 蔡少正 老師

Time: 2006/4/11 (16:00~16:50)        Place: Classroom 602


     Protein-nucleic acid interactions are responsible for the regulation of key biological functions such as transcription, translation, replication, and recombination. Nonspecific sites participate in the regulation of the physiological function because they complex, in vivo, most of the DNA binding protein molecules that are not bound at their regulatory functional sites. Nonspecific protein-DNA interactions speed up the search for the target site by several orders of magnitude. In this paper, they report the solution structure and dynamics of the complex of a dimeric lac repressor DNA binding domain with nonspecific DNA. The same set of residues can switch roles from a purely electrostatic interaction with the DNA backbone in the nonspecific complex to a highly specific binding mode with the base pairs of the cognate operator sequence. The protein-DNA interface of the nonspecific complex is flexible on biologically relevant time scales that may assist in the rapid and efficient binding of the target site.


1.      Charalampos G.Kalodimos. et al. Activation Function-1 Domain of Androgen Receptor Contributes to the Interaction between Subnuclear Splicing Factor Compartment and Nuclear Receptor Compartment. The EMBO journal. Vol. 21 No. 12 pp. 2866–2876, 2002