Open AccessProtein-protein interactions with the acidic COOH terminus of the single-stranded DNA-binding protein of the bacteriophage T4.
Author(s) -
Kathy Boltrek Krassa,
Louis S. Green,
Larry Gold
Publication year - 1991
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.88.9.4010
Subject(s) - microbiology and biotechnology , biology , hmg box , n terminus , seqa protein domain , dna , binding domain , single stranded binding protein , dna binding protein , ddb1 , c terminus , dna binding domain , epitope , dna replication , biochemistry , gene , binding site , peptide sequence , amino acid , transcription factor , antibody , origin of replication , genetics
The single-stranded DNA-binding protein of the bacteriophage T4 is encoded by gene 32. Monoclonal antibodies were raised against intact gene 32 protein (gp32). We mapped the epitopes recognized by 12 of these monoclonal antibodies; the epitopes are all within the COOH-terminal region of gp32. As shown by others, removal of the COOH terminus of gp32 abolishes the ability of the intact protein to bind to many T4 proteins involved in replication, recombination, repair, and late transcription. These results suggest that the COOH terminus of gp32 is a protein-binding domain. The COOH terminus is attached to a DNA-binding domain that includes a zinc finger. We propose a model in which the DNA-binding and protein-binding domains are used in T4 replication, recombination, repair, and late transcription. The COOH terminus of gp32 is very acidic and may form four negatively charged amphipathic alpha-helices, which could fold into a four-helix bundle when associated with other proteins. At least six of the monoclonal anti-gp32 antibodies bind to the COOH terminus of gp32 and to DNA. Similarities between the COOH terminus of gp32 and DNA are explored.