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The Bifunctional Primase‐Helicases of Bacteriophage T7 and Arabidopsis thaliana
Author(s) -
Crampton Donald J,
Richardson Charles C
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a513
Subject(s) - primase , helicase , biology , rna helicase a , arabidopsis thaliana , dna , arabidopsis , bacteriophage , gene , biochemistry , translocase , dna replication , microbiology and biotechnology , rna , reverse transcriptase , escherichia coli , mutant , chromosomal translocation
The primase and helicase activities of most organisms reside in separate but interacting proteins. By contrast, in the bacteriophage T7 gene 4 protein, these activities are in a single polypeptide. The N‐terminal primase domain is responsible for template‐directed oligoribonucleotide synthesis whereas the C‐terminal helicase domain is responsible for helicase‐associated activities such as oligomer formation, DNA‐dependent dTTP hydrolysis, and translocation along single‐stranded DNA. Arabidopsis thaliana possesses a homolog of T7 gene 4 protein. The Arabidopsis protein has primary sequence similarity to the T7 gene 4 protein, but no specific enzyme activity has been observed up to now. Sequence analysis of the N‐terminus indicates that the protein is targeted to the mitochondria suggesting a possible relationship between the DNA replication in bacteriophages and plant mitochondria.