RPA subunit arrangement near the 3′-end of the primer is modulated by the length of the template strand and cooperative protein interactions

To analyze the interaction of human replication protein A (RPA) and its subunits with the DNA template-primer junction in the DNA replication fork, we designed several template-primer systems differing in the size of the single-stranded template tail (4, 9, 13, 14,19 and 31 nt). Base substituted pho...

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Veröffentlicht in:	Nucleic acids research 1999-11, Vol.27 (21), p.4235-4240
Hauptverfasser:	Lavrik, Olga I., Kolpashchikov, Dmitry M., Weisshart, Klaus, Nasheuer, Heinz-Peter, Khodyreva, Svetlana N., Favre, Alain
Format:	Artikel
Sprache:	eng
Schlagworte:	Azides - chemistry Azides - metabolism Cross-Linking Reagents - chemistry Cross-Linking Reagents - metabolism DNA - biosynthesis DNA Helicases - chemistry DNA Helicases - metabolism DNA Polymerase beta - metabolism DNA Polymerase I - metabolism DNA Primers - genetics DNA Primers - metabolism DNA Replication - genetics DNA, Single-Stranded - chemistry DNA, Single-Stranded - genetics DNA, Single-Stranded - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Escherichia coli - enzymology Humans Models, Biological Molecular Weight p32 protein p70 protein Protein Binding Protein Conformation Replication Protein A Templates, Genetic Ultraviolet Rays Uridine Triphosphate - analogs & derivatives Uridine Triphosphate - chemistry Uridine Triphosphate - metabolism
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