-transparent.png){kind=logo}
The bacteriophage T4 dda protein is a 5'-3' DNA helicase that stimulates DNA replication and recombination reactions in vitro and seems to play a role in the initiation of T4 DNA replication in vivo. Oligonucleotide probes based on NH2-terminal amino acid sequence were used to precisely map the location of the dda gene on the T4 chromosome. Using polymerase chain reaction techniques, the dda gene was then cloned into an expression vector, and the overproduced protein was purified in two chromatography steps. Both the genomic and cloned dda genes were sequenced and found to be identical, encoding a protein of 439 amino acids. The dda protein contains amino acid sequences resembling those of other known helicases, and is most homologous to the Escherichia coli recD protein. Protein affinity chromatography was used to show a direct interaction between the dda protein and the T4 uvsX protein (a rec A-type DNA recombinase).
K J Hacker, and
B M Alberts
October 1984,
The Journal of biological chemistry,
K J Hacker, and
B M Alberts
January 2015,
DNA repair,
K J Hacker, and
B M Alberts
September 1995,
The Journal of biological chemistry,
K J Hacker, and
B M Alberts
August 2004,
The Journal of biological chemistry,
K J Hacker, and
B M Alberts
February 1994,
Biochemical and biophysical research communications,
K J Hacker, and
B M Alberts
March 1989,
The Journal of biological chemistry,
K J Hacker, and
B M Alberts
November 2002,
Proceedings of the National Academy of Sciences of the United States of America,
K J Hacker, and
B M Alberts
February 2002,
Nucleic acids research,
K J Hacker, and
B M Alberts
August 1983,
Cell,
K J Hacker, and
B M Alberts
October 2005,
Biochemistry,
