Electron microscopy of a eukaryotic single-stranded DNA binding protein-DNA complex

Banks, Geoffrey R.; Spanos, Ad; Kairis, Michael V.; Molineux, Ian J.

doi:10.1016/0022-2836(81)90519-2

Cited by 4 publications

(1 citation statement)

References 22 publications

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“…The purified T7 DNA binding protein has a large repertoire of functions that include its ability to bind cooperatively to single-stranded DNA (Banks et al, 1981), to stimulate the T7 DNA polymerase (Scherzinger et al, 1973;Reuben & Gefter, 1973), and to promote renaturation of DNA (Sadowski et al, 1980). We have focused in this paper on its ability to stimulate specifically the activity of the gene 6 exonuclease in the presence of moderate concentrations of salt.…”

Section: Discussionmentioning

confidence: 99%

Specific stimulation of the T7 gene 6 exonuclease by the phage T7 coded deoxyribonucleic acid binding protein

Roberts¹,

Sadowski²,

Wong³

1982

Biochemistry

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Bacteriophage T7 codes for a single-stranded DNA binding protein. This protein is the product of gene 2.5 and has been found previously to stimulate specifically the activity of the phage-coded DNA polymerase. We report here that the T7 DNA binding protein also stimulates the activity of the phage-coded exonuclease. The gene 6 exonuclease is a double-stranded DNA specific 5'-exonuclease that has been implicated in destruction of bacterial DNA, removal of RNA primers during DNA replication, genetic recombination, and DNA maturation. The enzyme is markedly inhibited by physiological concentrations of NaCl. This inhibition, which is due to a marked reduction in the Vmax of the enzyme, can be largely overcome by the phage-coded DNA binding protein. This stimulation is specific since the Escherichia coli DNA binding protein is without effect. The stimulation by the binding protein is apparently not due to its coating of the 3' single-stranded tails generated during the digestion. Kinetic studies show that the stimulation is due to a combined effect on both the Km and Vmax of the exonuclease. These studies are consistent with a loose binding of the binding protein to either the DNA or the exonuclease.

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Section: Discussionmentioning

confidence: 99%

Specific stimulation of the T7 gene 6 exonuclease by the phage T7 coded deoxyribonucleic acid binding protein

Roberts¹,

Sadowski²,

Wong³

1982

Biochemistry

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

Meyer

Thomas

Koerner

et al. 1984

Advances in Experimental Medicine and Biology

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Age‐dependent changes in the level of a 34 kDa DNA‐binding protein in developing chick embryo liver

David

Shanmugam

1985

FEBS Letters

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The relative amounts of a DNA-binding protein of 34 kDa increased during the early stages of development of chick embryo liver. The content of this protein reached a maximum in 18-19-day-old embryonic livers and decreased afterwards in older embryonic and post-natal chick livers. The 34 kDa polypeptide is the major DNA-binding protein (DBP) of embryonic liver and it preferentially binds to single-stranded DNA.The quantity of the 34 kDa DBP was relatively very low in embryonic muscle, heart and brain.

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Electron microscopy of a eukaryotic single-stranded DNA binding protein-DNA complex

Cited by 4 publications

References 22 publications

Specific stimulation of the T7 gene 6 exonuclease by the phage T7 coded deoxyribonucleic acid binding protein

Specific stimulation of the T7 gene 6 exonuclease by the phage T7 coded deoxyribonucleic acid binding protein

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

Age‐dependent changes in the level of a 34 kDa DNA‐binding protein in developing chick embryo liver

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