The primosomal protein n' of Escherichia coli is a DNA helicase - PubMed (original) (raw)
. 1988 Apr 25;263(12):5512-8.
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- PMID: 2833507
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The primosomal protein n' of Escherichia coli is a DNA helicase
R S Lasken et al. J Biol Chem. 1988.
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Abstract
Protein n' of Escherichia coli functions in assembly and translocation of the primosome, a mobile multiprotein complex involved in priming DNA replication (Kornberg, A. (1982) Supplement to DNA Replication, Freeman Publications, San Francisco). By itself, protein n' translocates on single-stranded DNA and destabilizes duplex regions by acting as a DNA helicase, using the energy of ATP or dATP hydrolysis. Single-stranded DNA binding protein was required for melting of duplex regions longer than 40 base pairs. Initial binding of protein n' to a specific site on DNA (Shlomai, J., and Kornberg, A. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 799-803) is essential for its helicase function. The polarity of protein n' translocation on DNA, in the 3' to 5' direction of the chain, suggests a mechanism for how the primosome may contribute to concurrent replication of both strands at a replication fork.
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