E. coli single-strand DNA bind

单链结合蛋白 single strand binding protein

这种蛋白又称为双螺旋稳定蛋白（helix destabilizing protein）。当解旋酶将双链打开以后，单链DNA具有一种潜在的恢复原来双链的能力，重新形成氢键。而且单链本身若有反向重复也会形成发夹结构，这两种情况都会影响复制的，但SSB可以解决这一问题。SSB并不是酶，是由177个aa组成的蛋白，E.coli 的SSB以四聚存在，分子量为74KDa，结合在单链上，每个分子可以覆盖32Nt，使DNA受到保护，不被酶水解，也不回复成双链，因此可以降低DNA的Tm值。SSB

Screening Peptide/Protein Libraries Fused to the Repressor DNA-Binding Domain in E. coli Cells

The use of λ repressor fusions to study protein-protein interactions in E. coli was first described by Hu and others ( 1 ). Since then, the repressor system has been employed by several laboratories to screen

Cloning of HIV Single-Strand DNA Binding Protein from Human Lymphocyte Lambda gt11 Expression Library with [32P]-Oligomers

(antigens) are expressed as a β-galactosidase fusion protein in E. coli . Because the lacZ gene has a strong promoter, the fusion proteins comprise from 0.1–4% of the total E. coli proteins (1 –3 ). The expressed fusion antigens are transferred