Interaction of DNA polymerase α-primase with cellular replication protein A and SV40 T antigen

I. Dornreiter; L. F. Erdile; L. U. Gilbert; D. Von Winkler; T. J. Kelly; E. Fanning

doi:10.1002/j.1460-2075.1992.tb05110.x

Interaction of DNA polymerase α-primase with cellular replication protein A and SV40 T antigen

I. Dornreiter, L. F. Erdile, L. U. Gilbert, D. Von Winkler, T. J. Kelly, E. Fanning

Research output: Contribution to journal › Article › peer-review

275 Scopus citations

Abstract

The purified human single-stranded DNA binding protein, replication protein A (RP-A), forms specific complexes with purified SV40 large T antigen and with purified DNA polymerase α-primase, as shown by ELISA and a modified immunoblotting technique, RP-A associated efficiently with the isolated primase, as well as with intact polymerase α-primase. The 70 kDa subunit of RP-A was sufficient for association with polymerase α-primase. Purified SV40 large T antigen bound to intact RP-A and to polymerase-primase, but not to any of the separated subunits of RP-A or to the isolated primase. These results suggest that the specific protein-protein interactions between RP-A, polymerase-primase and T antigen may play a role in the initiation of SV40 DNA replication.

Original language	English (US)
Pages (from-to)	769-776
Number of pages	8
Journal	EMBO Journal
Volume	11
Issue number	2
DOIs	https://doi.org/10.1002/j.1460-2075.1992.tb05110.x
State	Published - 1992
Externally published	Yes

Keywords

DNA polymerase α
Initiation of DNA replication
Protein-protein interactions
SV40 T antigen
Single-strand DNA binding protein

ASJC Scopus subject areas

Neuroscience(all)
Molecular Biology
Biochemistry, Genetics and Molecular Biology(all)
Immunology and Microbiology(all)

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10.1002/j.1460-2075.1992.tb05110.x

Cite this

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title = "Interaction of DNA polymerase α-primase with cellular replication protein A and SV40 T antigen",

abstract = "The purified human single-stranded DNA binding protein, replication protein A (RP-A), forms specific complexes with purified SV40 large T antigen and with purified DNA polymerase α-primase, as shown by ELISA and a modified immunoblotting technique, RP-A associated efficiently with the isolated primase, as well as with intact polymerase α-primase. The 70 kDa subunit of RP-A was sufficient for association with polymerase α-primase. Purified SV40 large T antigen bound to intact RP-A and to polymerase-primase, but not to any of the separated subunits of RP-A or to the isolated primase. These results suggest that the specific protein-protein interactions between RP-A, polymerase-primase and T antigen may play a role in the initiation of SV40 DNA replication.",

keywords = "DNA polymerase α, Initiation of DNA replication, Protein-protein interactions, SV40 T antigen, Single-strand DNA binding protein",

author = "I. Dornreiter and Erdile, {L. F.} and Gilbert, {L. U.} and {Von Winkler}, D. and Kelly, {T. J.} and E. Fanning",

year = "1992",

doi = "10.1002/j.1460-2075.1992.tb05110.x",

language = "English (US)",

volume = "11",

pages = "769--776",

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T1 - Interaction of DNA polymerase α-primase with cellular replication protein A and SV40 T antigen

AU - Dornreiter, I.

AU - Erdile, L. F.

AU - Gilbert, L. U.

AU - Von Winkler, D.

AU - Kelly, T. J.

AU - Fanning, E.

PY - 1992

Y1 - 1992

N2 - The purified human single-stranded DNA binding protein, replication protein A (RP-A), forms specific complexes with purified SV40 large T antigen and with purified DNA polymerase α-primase, as shown by ELISA and a modified immunoblotting technique, RP-A associated efficiently with the isolated primase, as well as with intact polymerase α-primase. The 70 kDa subunit of RP-A was sufficient for association with polymerase α-primase. Purified SV40 large T antigen bound to intact RP-A and to polymerase-primase, but not to any of the separated subunits of RP-A or to the isolated primase. These results suggest that the specific protein-protein interactions between RP-A, polymerase-primase and T antigen may play a role in the initiation of SV40 DNA replication.

AB - The purified human single-stranded DNA binding protein, replication protein A (RP-A), forms specific complexes with purified SV40 large T antigen and with purified DNA polymerase α-primase, as shown by ELISA and a modified immunoblotting technique, RP-A associated efficiently with the isolated primase, as well as with intact polymerase α-primase. The 70 kDa subunit of RP-A was sufficient for association with polymerase α-primase. Purified SV40 large T antigen bound to intact RP-A and to polymerase-primase, but not to any of the separated subunits of RP-A or to the isolated primase. These results suggest that the specific protein-protein interactions between RP-A, polymerase-primase and T antigen may play a role in the initiation of SV40 DNA replication.

KW - DNA polymerase α

KW - Initiation of DNA replication

KW - Protein-protein interactions

KW - SV40 T antigen

KW - Single-strand DNA binding protein

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Interaction of DNA polymerase α-primase with cellular replication protein A and SV40 T antigen

Abstract

Keywords

ASJC Scopus subject areas

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