Open AccessAffinity purification of bacteriophage T4 proteins essential for DNA replication and genetic recombination.
Author(s) -
Tim Formosa,
Rae Lyn Burke,
Bruce Alberts
Publication year - 1983
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.80.9.2442
Subject(s) - biology , bacteriophage , gene , dna , escherichia coli , genetic recombination , seqa protein domain , microbiology and biotechnology , dna replication , dna binding protein , affinity chromatography , genetics , biochemistry , origin of replication , recombination , enzyme , transcription factor
The bacteriophage T4 helix-destabilizing protein, the product of gene 32, has been immobilized on an agarose matrix and used for affinity chromatography of lysates of T4-infected Escherichia coli cells. At least 10 T4-encoded early proteins and 3 or 4 host proteins are specifically retained by this gene 32 protein column. Nine of the T4 proteins have been identified as being involved in either DNA replication or genetic recombination. Notably, the T4 DNA polymerase (gene 43 protein) and two major proteins in the recombination pathway (the products of genes uvsX and uvsY) are specifically bound. On a preparative scale, the column is useful for purification of the bound proteins.