Gene V protein of fd bacteriophage. Dimer formation and the role of tyrosyl groups in DNA binding.
作者： HT Pretorius , M Klein , LA Day
DOI: 10.1016/S0021-9258(19)40638-8
关键词: In vitro 、 Protein subunit 、 Crystallography 、 Dimer 、 Nucleotide 、 Gene 、 Monomer 、 Nucleobase 、 DNA 、 Chemistry
摘要: Gene V protein exists principally as a dimer in neutral buffers which are 0.15 M NaCl, NaF, or NaClO4. Higher concentrations of NaClO4 NaCl disrupt the dimers, but higher NaF do not. There is single sulfhydryl group per gene monomer native monomers, and DNA-protein complexes. Disulfide formation leads to loss solubility DNA binding capacity. The fluorescence tyrosyl groups same for monomers dimers solutions, it extensively quenched on poly(dT) fd-DNA. Complexes fd-DNA isolated from lysates infected cells were found contain 4.70- +/- 0.13 nucleotides whereas complexes formed vitro 4.05 0.17 nucleotides/monomer. It postulated that not involved protein-protein interactions monomer-dimer equilibrium, stack with bases complexes, each subunit intracellular replaced by exactly two subunits major coat during final assembly virus.
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