Interaction of DNA Accessory Proteins with DNA Polymerase β of the Novikoff Hepatoma

Meyer, Ralph R.; Thomas, David C.; Koerner, T J; Rein, Diane C.

doi:10.1007/978-1-4684-8730-5_37

Cited by 2 publications

(1 citation statement)

References 10 publications

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“…Proteins that must bind ssDNA to carry out their function are often inhibited by SSB, since such proteins have a lower affinity for ssDNA and cannot displace bound SSB. Many DNA-dependent ATPases that require a single-strand effector show inhibition of the ATPase activity by SSB and include Rep, n' (except on (X174 DNA), ATPase IV, RecA, helicase II, DnaB, and a variety of mammalian enzymes (8,13,90,95,98,186,245,247,256,258,262,352,382,383). Transcription is inhibited by SSB (288), as are most single-strand exo-and endonucleases (131, 234, 258, 270-272, 327, 387).…”

Section: Modulation Of Enzymatic Activities By Ssbmentioning

confidence: 99%

The single-stranded DNA-binding protein of Escherichia coli.

Meyer

Laine

1990

Microbiological Reviews

275

216

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Section: Modulation Of Enzymatic Activities By Ssbmentioning

confidence: 99%

The single-stranded DNA-binding protein of Escherichia coli.

Meyer

Laine

1990

Microbiological Reviews

275

216

View full text Add to dashboard Cite

The single-stranded DNA-binding protein of Escherichia coli

1990

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The single-stranded DNA-binding protein (SSB) of Escherichia coli is involved in all aspects of DNA metabolism: replication, repair, and recombination. In solution, the protein exists as a homotetramer of 18,843-kilodalton subunits. As it binds tightly and cooperatively to single-stranded DNA, it has become a prototypic model protein for studying protein-nucleic acid interactions. The sequences of the gene and protein are known, and the functional domains of subunit interaction, DNA binding, and protein-protein interactions have been probed by structure-function analyses of various mutations. The ssb gene has three promoters, one of which is inducible because it lies only two nucleotides from the LexA-binding site of the adjacent uvrA gene. Induction of the SOS response, however, does not lead to significant increases in SSB levels. The binding protein has several functions in DNA replication, including enhancement of helix destabilization by DNA helicases, prevention of reannealing of the single strands and protection from nuclease digestion, organization and stabilization of replication origins, primosome assembly, priming specificity, enhancement of replication fidelity, enhancement of polymerase processivity, and promotion of polymerase binding to the template. E. coli SSB is required for methyl-directed mismatch repair, induction of the SOS response, and recombinational repair. During recombination, SSB interacts with the RecBCD enzyme to find Chi sites, promotes binding of RecA protein, and promotes strand uptake.

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Interaction of DNA Accessory Proteins with DNA Polymerase β of the Novikoff Hepatoma

Cited by 2 publications

References 10 publications

The single-stranded DNA-binding protein of Escherichia coli.

The single-stranded DNA-binding protein of Escherichia coli.

The single-stranded DNA-binding protein of Escherichia coli

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