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The actin-like MreB cytoskeleton organizes viral DNA replication in bacteria.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2009 Aug 11; Vol. 106 (32), pp. 13347-52. - Publication Year :
- 2009
-
Abstract
- Little is known about the organization or proteins involved in membrane-associated replication of prokaryotic genomes. Here we show that the actin-like MreB cytoskeleton of the distantly related bacteria Escherichia coli and Bacillus subtilis is required for efficient viral DNA replication. Detailed analyses of B. subtilis phage ϕ29 showed that the MreB cytoskeleton plays a crucial role in organizing phage DNA replication at the membrane. Thus, phage double-stranded DNA and components of the ϕ29 replication machinery localize in peripheral helix-like structures in a cytoskeleton-dependent way. Importantly, we show that MreB interacts directly with the ϕ29 membrane-protein p16.7, responsible for attaching viral DNA at the cell membrane. Altogether, the results reveal another function for the MreB cytoskeleton and describe a mechanism by which viral DNA replication is organized at the bacterial membrane.
- Subjects :
- Actin Cytoskeleton genetics
Bacillus Phages genetics
Bacillus subtilis genetics
Bacterial Proteins genetics
Bacteriophage PRD1 genetics
Bacteriophage PRD1 physiology
Cell Membrane metabolism
Cell Membrane virology
DNA Replication genetics
DNA, Viral biosynthesis
DNA, Viral genetics
Escherichia coli genetics
Escherichia coli metabolism
Escherichia coli virology
Escherichia coli Proteins genetics
Escherichia coli Proteins metabolism
Genes, Bacterial
Membrane Proteins genetics
Membrane Proteins metabolism
Models, Biological
Mutation
Viral Proteins genetics
Viral Proteins metabolism
Virus Attachment
Virus Replication genetics
Actin Cytoskeleton metabolism
Bacillus Phages physiology
Bacillus subtilis metabolism
Bacillus subtilis virology
Bacterial Proteins metabolism
DNA Replication physiology
Virus Replication physiology
Subjects
Details
- Language :
- English
- ISSN :
- 1091-6490
- Volume :
- 106
- Issue :
- 32
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 19654094
- Full Text :
- https://doi.org/10.1073/pnas.0906465106