Escherichia coli replication factor Y, a component of the primosome, can act as a DNA helicase Journal Article


Authors: Lee, M. S.; Marians, K. J.
Article Title: Escherichia coli replication factor Y, a component of the primosome, can act as a DNA helicase
Abstract: The primosome is a mobile multienzyme DNA replication-priming complex that requires seven Escherichia coli proteins for assembly (the products of the dnaB, dnaC, dnaG, and dnaT genes as well as proteins n and n" and replication factor Y). It has been shown previously that the primosome, in combination with the E. coli DNA polymerase III holoenzyme, can form replication forks in vitro that move at rates similar to those measured in vivo and that the primosome and one of the components of the primosome, the DNA B protein, have DNA helicase activity. Evidence is presented here that another component of the primosome, replication factor Y, possesses DNA helicase activity as well. Factor Y helicase activity requires the presence of E. coli single-stranded DNA binding protein, Mg2+, and hydrolyzable ATP or dATP. Helicase activity is stimulated 15-fold when the enzyme is actively loaded onto single-stranded DNA through a primosome assembly site, and duplex DNA is unwound unidirectionally, 3'----5', along the DNA strand to which the protein is bound.
Keywords: dna binding protein; genetics; dna-binding proteins; dna replication; physiology; binding site; binding sites; helicase; single stranded dna; dna, single-stranded; multienzyme complex; multienzyme complexes; adenosine triphosphatase; adenosine triphosphatases; dna helicases; regulatory sequences, nucleic acid; regulatory sequence; dnab helicases; article; dnab helicase; dnab protein, e coli
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 84
Issue: 23
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1987-12-01
Start Page: 8345
End Page: 8349
Language: English
DOI: 10.1073/pnas.84.23.8345
PUBMED: 2825188
PROVIDER: scopus
PMCID: PMC299539
DOI/URL:
Notes: Article -- Export Date: 5 February 2021 -- Source: Scopus
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  1. Kenneth Marians
    127 Marians