Authors: | Liu, J.; Nurse, P.; Marians, K. J. |
Article Title: | The ordered assembly of the φX174-type primosome: III. PriB facilitates complex formation between PriA and DnaT |
Abstract: | The properties of two mutant PriA proteins, PriA C439Y and PriA C445Y have been used to reveal the role of PriB during assembly of the φX174-type primosome. The replication defects of both mutant PriA proteins could be rescued by high concentrations of DnaT. Analysis of the formation of intermediate complexes in primosome assembly and the effect of PriB on PriA binding to DNA demonstrated that the mutant PriA proteins could not form a PriA-PriB complex on DNA carrying a primosome assembly site. Consequently, the mutant proteins also could not form PriA-PriB-DnaT complexes at concentrations of DnaT sufficient to form such a complex with wild-type PriA. In addition, PriB was found to stabilize wild-type but not mutant PriA proteins on DNA. At high concentrations of DnaT, both mutant and wild-type PriA proteins could form a PriA-DnaT complex and support PriB-independent φX174 complementary strand DNA replication. Thus, during primosome assembly, PriB facilitates complex formation between PriA and DnaT. |
Keywords: | dna binding protein; genetics; dna-binding proteins; nonhuman; dna replication; metabolism; protein assembly; structure activity relation; structure-activity relationship; bacterial protein; bacterial proteins; protein processing; escherichia coli; binding site; dna, viral; mutagenesis, site-directed; single stranded dna; dna, single-stranded; site directed mutagenesis; protein determination; escherichia coli proteins; macromolecule; macromolecular substances; virus dna; escherichia coli protein; dna protein complex; bacteriophage phi x 174; priority journal; article; prib protein, e coli |
Journal Title: | Journal of Biological Chemistry |
Volume: | 271 |
Issue: | 26 |
ISSN: | 0021-9258 |
Publisher: | American Society for Biochemistry and Molecular Biology |
Date Published: | 1996-06-28 |
Start Page: | 15656 |
End Page: | 15661 |
Language: | English |
DOI: | 10.1074/jbc.271.26.15656 |
PUBMED: | 8663106 |
PROVIDER: | scopus |
DOI/URL: | |
Notes: | Article -- Export Date: 22 November 2017 -- Source: Scopus |