Faculty Opinions recommendation of Intrinsically disordered C-terminal tails of E. coli single-stranded DNA binding protein regulate cooperative binding to single-stranded DNA.

ABSTRACT Bacteriophage P1 encodes a single-stranded DNA-binding protein (SSB-P1), which shows 66% amino acid sequence identity to the SSB protein of the host bacterium Escherichia coli. A phylogenetic analysis indicated that the P1 ssb gene coexists with its E. coli counterpart as an independent unit and does not represent a recent acquirement of the phage. The P1 and E. coli SSB proteins are fully functionally interchangeable. SSB-P1 is nonessential for phage growth in an exponentially growing E. coli host, and it is sufficient to promote bacterial growth in the absence of the E. coli SSB protein. Expression studies showed that the P1 ssb gene is transcribed only, in an rpoS-independent fashion, during stationary-phase growth in E. coli. Mixed infection experiments demonstrated that a wild-type phage has a selective advantage over an ssb-null mutant when exposed to a bacterial host in the stationary phase. These results reconciled the observed evolutionary conservation with the seemingly redundant presence of ssb genes in many bacteriophages and conjugative plasmids.

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Interaction of the E. coli single-stranded DNA-binding protein with nucleic acids and its comparison with protamine

10.31979/etd.qp6w-v894 ◽

1995 ◽

Author(s):

Shirin W Hasan

Keyword(s):

Dna Binding ◽

Nucleic Acids ◽

Binding Protein ◽

Dna Binding Protein ◽

Single Stranded Dna ◽

E Coli

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Decision letter: Structural dynamics of E. coli single-stranded DNA binding protein reveal DNA wrapping and unwrapping pathways

10.7554/elife.08193.023 ◽

2015 ◽

Keyword(s):

Dna Binding ◽

Structural Dynamics ◽

Binding Protein ◽

Dna Binding Protein ◽

Single Stranded Dna ◽

E Coli ◽

Dna Wrapping

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Author response: Structural dynamics of E. coli single-stranded DNA binding protein reveal DNA wrapping and unwrapping pathways

10.7554/elife.08193.024 ◽

2015 ◽

Author(s):

Sukrit Suksombat ◽

Rustem Khafizov ◽

Alexander G Kozlov ◽

Timothy M Lohman ◽

Yann R Chemla

Keyword(s):

Dna Binding ◽

Structural Dynamics ◽

Binding Protein ◽

Dna Binding Protein ◽

Author Response ◽

Single Stranded Dna ◽

E Coli ◽

Dna Wrapping

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The role of gene A protein and E. coli rep protein in the replication of ɸX 174 replicative form DNA

Proceedings of the Royal Society of London Series B Biological Sciences ◽

10.1098/rspb.1980.0138 ◽

1980 ◽

Vol 210 (1180) ◽

pp. 337-349 ◽

Cited By ~ 1

Keyword(s):

Dna Binding ◽

Dna Polymerase ◽

Binding Protein ◽

Dna Binding Protein ◽

Origin Of Replication ◽

Electron Microscopic ◽

Single Stranded Dna ◽

Rep Protein ◽

E Coli

The gene A protein of bacteriophage ɸX 174 initiates replication of super-twisted RFI DNA by cleaving the viral (+) strand at the origin of replication and binding to the 5' end. Upon addition of E. coli rep protein (single-stranded DNA dependent ATPase), E. coli single-stranded DNA binding protein and ATP, complete unwinding of the two strands occurs. Electron microscopic analyses of intermediates in the reaction reveal that the unwinding occurs by movement of the 5' end into the duplex, displacing the viral strand in the form of a single-stranded loop. Since unwinding will not occur in the absence of either gene A protein or rep protein, it is presumed that the rep protein interacts to form a complex with the bound gene A protein. Single-stranded DNA binding protein facilitates the unwinding by binding to the exposed single-stranded DNA. Further addition of the four deoxyribotriphosphates and DNA polymerase III holoenzyme to the reaction results in synthesis of viral (+) single-stranded circles in amounts exceeding that of the input template. A model describing the role of gene A protein and rep protein in duplex DNA replication is presented and other properties of gene A protein discussed.

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