Direct physical interaction between DnaG primase and DnaB helicase of Escherichia coli is necessary for optimal synthesis of primer RNA
Autor: | Deepak Bastia, Ya Bin Lu, Bidyut K. Mohanty, Pillarisetty V. A. L. Ratnakar |
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Rok vydání: | 1996 |
Předmět: |
DNA Replication
Transcription Genetic Molecular Sequence Data DNA Primase Primosome DnaG Open Reading Frames Bacterial Proteins Escherichia coli Point Mutation Amino Acid Sequence dnaB helicase Genetics Multidisciplinary Binding Sites biology DNA replication DNA Helicases Helicase RNA RNA Nucleotidyltransferases Biological Sciences Recombinant Proteins Kinetics RNA Bacterial Biochemistry Protein Biosynthesis biology.protein Mutagenesis Site-Directed bacteria Primase Primer (molecular biology) DnaB Helicases Protein Binding |
Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 93(23) |
ISSN: | 0027-8424 |
Popis: | The primase DnaG of Escherichia coli requires the participation of the replicative helicase DnaB for optimal synthesis of primer RNA for lagging strand replication. However, previous studies had not determined whether the activation of the primase or its loading on the template was accomplished by a helicase-mediated structural alteration of the single-stranded DNA or by a direct physical interaction between the DnaB and the DnaG proteins. In this paper we present evidence supporting direct interaction between the two proteins. We have mapped the surfaces of interaction on both DnaG and DnaB and show further that mutations that reduce the physical interaction also cause a significant reduction in primer synthesis. Thus, the physical interaction reported here appears to be physiologically significant. |
Databáze: | OpenAIRE |
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