Mutant DnaA proteins defective in duplex opening of oriC, the origin of chromosomal DNA replication in Escherichia coli

We characterized three mutant DnaA proteins with an amino acid substitution of R334H, R342H and E361G that renders chromosomal replication cold (20°C) sensitive. Each mutant DnaA protein was highly purified from overproducers, and replication activities were assayed in in vitro oriC replication syst...

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Veröffentlicht in:	Molecular microbiology 2000-01, Vol.35 (2), p.454-462
Hauptverfasser:	Takata, Makoto, Guo, Lei, Katayama, Tsutomu, Hase, Masakazu, Seyama, Yousuke, Miki, Takeyoshi, Sekimizu, Kazuhisa
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Bacterial Proteins - genetics Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Cold Temperature DNA Replication DNA-Binding Proteins - genetics DNA-Binding Proteins - isolation & purification DNA-Binding Proteins - metabolism DnaA protein Escherichia coli Escherichia coli - genetics Escherichia coli - growth & development Mutation Origin Recognition Complex replication origins Single-Strand Specific DNA and RNA Endonucleases - metabolism Viral Proteins - genetics Viral Proteins - metabolism
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