Mechanism of Recruitment of DnaB Helicase to the Replication Origin of the Plasmid pSC101
Although many bacterial chromosomes require only one replication initiator protein, e.g., DnaA, most plasmid replicons depend on dual initiators: host-encoded DnaA and plasmid-encoded Rep initiator protein for replication initiation. Using the plasmid pSC101 as a model system, this work investigates...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1999-01, Vol.96 (1), p.73-78 |
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| creator | Datta, Hirock J. Khatri, Ghan Shyam Bastia, Deepak |
| description | Although many bacterial chromosomes require only one replication initiator protein, e.g., DnaA, most plasmid replicons depend on dual initiators: host-encoded DnaA and plasmid-encoded Rep initiator protein for replication initiation. Using the plasmid pSC101 as a model system, this work investigates the biological rationale for the requirement for dual initiators and shows that the plasmid-encoded RepA specifically interacts with the replicative helicase DnaB. Mutations in DnaB or RepA that disrupt RepA-DnaB interaction cause failure to load DnaB to the plasmid ori in vitro and to replicate the plasmid in vivo. Although, interaction of DnaA with DnaB could not substitute for RepA-DnaB interaction for helicase loading, DnaA along with integration host factor, DnaC, and RepA was essential for helicase loading. Therefore, DnaA is indirectly needed for helicase loading. Instead of a common surface of interaction with initiator proteins, interestingly, DnaB helicase appears to have at least a limited number of nonoverlapping surfaces, each of which interacts specifically with a different initiator protein. |
| doi_str_mv | 10.1073/pnas.96.1.73 |
| format | Article |
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Using the plasmid pSC101 as a model system, this work investigates the biological rationale for the requirement for dual initiators and shows that the plasmid-encoded RepA specifically interacts with the replicative helicase DnaB. Mutations in DnaB or RepA that disrupt RepA-DnaB interaction cause failure to load DnaB to the plasmid ori in vitro and to replicate the plasmid in vivo. Although, interaction of DnaA with DnaB could not substitute for RepA-DnaB interaction for helicase loading, DnaA along with integration host factor, DnaC, and RepA was essential for helicase loading. Therefore, DnaA is indirectly needed for helicase loading. 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Using the plasmid pSC101 as a model system, this work investigates the biological rationale for the requirement for dual initiators and shows that the plasmid-encoded RepA specifically interacts with the replicative helicase DnaB. Mutations in DnaB or RepA that disrupt RepA-DnaB interaction cause failure to load DnaB to the plasmid ori in vitro and to replicate the plasmid in vivo. Although, interaction of DnaA with DnaB could not substitute for RepA-DnaB interaction for helicase loading, DnaA along with integration host factor, DnaC, and RepA was essential for helicase loading. Therefore, DnaA is indirectly needed for helicase loading. Instead of a common surface of interaction with initiator proteins, interestingly, DnaB helicase appears to have at least a limited number of nonoverlapping surfaces, each of which interacts specifically with a different initiator protein.</description><subject>Bacteria</subject><subject>Bacterial Proteins</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Codons</subject><subject>Coordinate systems</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA Helicases - metabolism</subject><subject>DNA Replication</subject><subject>DNA, Bacterial - biosynthesis</subject><subject>DNA-Binding Proteins</subject><subject>DnaB Helicases</subject><subject>Genetic mutation</subject><subject>Models, Genetic</subject><subject>Mutagenesis, Site-Directed</subject><subject>Nucleotides</subject><subject>Plasmids</subject><subject>Plasmids - biosynthesis</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Proteins - genetics</subject><subject>Proteins - metabolism</subject><subject>Replicon</subject><subject>Trans-Activators</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kUur1DAYhoMox_HozpUiFBFXdvxyadOAGx0vRzhyxMvCVUjT9EyGNqlJKvrvTZmhqOAqJM_zhjf5ELqPYYuB0-eTU3Er6i3ecnoDbTAIXNZMwE20ASC8bBhht9GdGA8AIKoGztCZaDjjnG3Qtw9G75WzcSx8X3wyOsw2jcalZfvaqVfFhRmsVtEUyRdpb7IzLQfJeldcBXtt3aIu5OOg4mi7Yvq8w4Dvolu9GqK5d1rP0de3b77sLsrLq3fvdy8vS10BTSURrcKs76umIZ3gbUOYqqve6K5RooeWVIQ3tFetqnmrNQCvADrFcEspUMPoOXpxvHea29F0OncPapBTsKMKv6RXVv5NnN3La_9D4ir_Ro4_PcWD_z6bmORoozbDoJzxc5SYY9pUdZ3Fx_-IBz8Hl58mCWBKBKM4S8-Okg4-xmD6tQcGuUxLLtOSopZYcpr1R392X-XTeDJ_eOJLaqVr-sn_qeznYUjmZ8rag6N2iMmH1WMcE0Z_A8J7r9Q</recordid><startdate>19990105</startdate><enddate>19990105</enddate><creator>Datta, Hirock J.</creator><creator>Khatri, Ghan Shyam</creator><creator>Bastia, Deepak</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><general>The National Academy of Sciences</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>19990105</creationdate><title>Mechanism of Recruitment of DnaB Helicase to the Replication Origin of the Plasmid pSC101</title><author>Datta, Hirock J. ; Khatri, Ghan Shyam ; Bastia, Deepak</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c503t-29ba14ff5882d97b824a65fecd8a9f0b252783faba67bcc007500da41b3303e43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Bacteria</topic><topic>Bacterial Proteins</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biological Sciences</topic><topic>Codons</topic><topic>Coordinate systems</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA Helicases - metabolism</topic><topic>DNA Replication</topic><topic>DNA, Bacterial - biosynthesis</topic><topic>DNA-Binding Proteins</topic><topic>DnaB Helicases</topic><topic>Genetic mutation</topic><topic>Models, Genetic</topic><topic>Mutagenesis, Site-Directed</topic><topic>Nucleotides</topic><topic>Plasmids</topic><topic>Plasmids - biosynthesis</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Proteins - genetics</topic><topic>Proteins - metabolism</topic><topic>Replicon</topic><topic>Trans-Activators</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Datta, Hirock J.</creatorcontrib><creatorcontrib>Khatri, Ghan Shyam</creatorcontrib><creatorcontrib>Bastia, Deepak</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Datta, Hirock J.</au><au>Khatri, Ghan Shyam</au><au>Bastia, Deepak</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mechanism of Recruitment of DnaB Helicase to the Replication Origin of the Plasmid pSC101</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1999-01-05</date><risdate>1999</risdate><volume>96</volume><issue>1</issue><spage>73</spage><epage>78</epage><pages>73-78</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Although many bacterial chromosomes require only one replication initiator protein, e.g., DnaA, most plasmid replicons depend on dual initiators: host-encoded DnaA and plasmid-encoded Rep initiator protein for replication initiation. Using the plasmid pSC101 as a model system, this work investigates the biological rationale for the requirement for dual initiators and shows that the plasmid-encoded RepA specifically interacts with the replicative helicase DnaB. Mutations in DnaB or RepA that disrupt RepA-DnaB interaction cause failure to load DnaB to the plasmid ori in vitro and to replicate the plasmid in vivo. Although, interaction of DnaA with DnaB could not substitute for RepA-DnaB interaction for helicase loading, DnaA along with integration host factor, DnaC, and RepA was essential for helicase loading. Therefore, DnaA is indirectly needed for helicase loading. 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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1999-01, Vol.96 (1), p.73-78 |
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| subjects | Bacteria Bacterial Proteins Binding Sites Biochemistry Biological Sciences Codons Coordinate systems Deoxyribonucleic acid DNA DNA Helicases - metabolism DNA Replication DNA, Bacterial - biosynthesis DNA-Binding Proteins DnaB Helicases Genetic mutation Models, Genetic Mutagenesis, Site-Directed Nucleotides Plasmids Plasmids - biosynthesis Protein Binding Proteins Proteins - genetics Proteins - metabolism Replicon Trans-Activators |
| title | Mechanism of Recruitment of DnaB Helicase to the Replication Origin of the Plasmid pSC101 |
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