Disease relevance of T7p24

• The helicase and primase activities of bacteriophage T7 are distributed between the 56- and 63-kDa gene 4 proteins [1].
• The helicase domain of the replicative helicase-primase protein from bacteriophage T7 crystallized as a helical filament that resembles the Escherichia coli RecA protein, an ATP-dependent DNA strand exchange factor [2].

High impact information on T7p24

• The structural mechanism of translocation and helicase activity in T7 RNA polymerase [3].
• DNA-induced switch from independent to sequential dTTP hydrolysis in the bacteriophage T7 DNA helicase [4].
• The replisome consisting of bacteriophage T7 DNA polymerase, helicase, primase, and single-stranded DNA-binding protein mediates coordinated replication [5].
• Single-stranded DNA binding protein and DNA helicase of bacteriophage T7 mediate homologous DNA strand exchange [6].
• Bacteriophage T7 helicase functions as a hexameric ring to drive the replication complex by separating the DNA strands during genome replication [7].

Chemical compound and disease context of T7p24

• The arginine finger of bacteriophage T7 gene 4 helicase: role in energy coupling [8].
• Gene 4 helicase of bacteriophage T7 mediates strand transfer through pyrimidine dimers, mismatches, and nonhomologous regions [9].
• Leading and lagging strand synthesis at the replication fork of bacteriophage T7. Distinct properties of T7 gene 4 protein as a helicase and primase [10].

Biological context of T7p24

• T7 gene 4, which is required for DNA replication, specifies two proteins whose coding sequences overlap in the same reading frame: the 4A protein, a 566-amino acid primase/helicase, and the 4B protein, a 503-amino acid helicase whose initiation codon is the 64th codon of the 4A protein [11].
• Thus, DNA helicase is able to participate in recombinational DNA repair through its role in strand exchange, providing a pathway distinct from nucleotide excision repair [9].
• The nucleotide binding site of the helicase/primase of bacteriophage T7. Interaction of mutant and wild-type proteins [12].
• Mutations in the C-terminal half clustered in or near five helicase consensus sequences [13].
• A complex presumably consisting of T7 DNA polymerase and gene 4 helicase/primase molecules was present at the fork together with a variable amount of single-stranded DNA sequestered by gene 2.5 single-stranded DNA binding protein [14].

Associations of T7p24 with chemical compounds

• The crystal structure of the hexameric helicase shows Arg-522, located at the subunit interface, positioned to interact with the gamma-phosphate of bound nucleoside 5' triphosphate [8].
• The 4A' gene, which has a leucine codon replacing the 4B initiation codon, specifies a single 566-amino acid protein that can provide the primase and helicase functions required for normal T7 growth [13].

Regulatory relationships of T7p24

• The T7 gene 4 protein acts processively as helicase to promote leading strand synthesis and distributively as primase to initiate lagging strand synthesis by T7 DNA polymerase [15].

Analytical, diagnostic and therapeutic context of T7p24

• The oligomeric structure of bacteriophage T7 gene 4 helicase/primase proteins was investigated using protein cross-linking and high pressure gel-filtration chromatography [16].
• Complementation tests with partially and completely defective phage showed that all but five of the mutants lacked helicase function but retained primase function [13].
• Characterization and crystallization of the helicase domain of bacteriophage T7 gene 4 protein [17].

References