Two modes of PriA binding to DNA Journal Article
| Authors: | Nurse, P.; Liu, J.; Marians, K. J. |
| Article Title: | Two modes of PriA binding to DNA |
| Abstract: | The role of PriA, required for the assembly of the φX174-type primosome on DNA, in cellular DNA replication has been unclear since its discovery. Recent evidence, based on the phenotypes of strains carrying priA null mutations, has led to proposals that the primosome assembly activity of PriA was required to load replication forks at intermediates such as D loops during homologous recombination. McGlynn et al. (McGlynn, P., Al-Deib, A. A., Liu, J., Marians, K. J., and Lloyd, R. G. (1997) J. Mol. Biol. 270, 212-221) demonstrated that PriA could, in fact, bind D loops. We show here that there are two modes of stable binding of PriA to DNA. One mode, in which the enzyme binds 3'-single-stranded extensions from duplex DNAs, presumably reflects the 3' → 5' DNA helicase activity of PriA. The D loop DNA binding activity of PriA can be accounted for by the second mode, where the enzyme binds bent DNA at three strand junctions. |
| Keywords: | unclassified drug; dna-binding proteins; dna replication; dna recombination; protein dna binding; molecular dynamics; enzyme activity; dna; double stranded dna; helicase; nucleic acid conformation; enzyme specificity; adenosine triphosphatases; dna determination; reaction analysis; dna helicases; concentration response; oligodeoxynucleotide; electrophoresis, polyacrylamide gel; oligodeoxyribonucleotides; dna conformation; dna strand; binding kinetics; priority journal; article; enzyme pria |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 274 |
| Issue: | 35 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 1999-08-27 |
| Start Page: | 25026 |
| End Page: | 25032 |
| Language: | English |
| DOI: | 10.1074/jbc.274.35.25026 |
| PUBMED: | 10455181 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 16 August 2016 -- Source: Scopus |
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