SV40 DNA Replication

1992 ◽  
pp. 129-158 ◽  
Author(s):  
T. Melendy ◽  
B. Stillman
Keyword(s):  
Dna Replication ◽  
Sv40 Dna

scholarly journals Termination complex in Escherichia coli inhibits SV40 DNA replication in vitro by impeding the action of T antigen helicase.

1992 ◽  
Vol 267 (8) ◽  
pp. 5361-5365
Author(s):  
M Hidaka ◽  
T Kobayashi ◽  
Y Ishimi ◽  
M Seki ◽  
T Enomoto ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Dna Replication ◽  
T Antigen ◽  
Sv40 Dna

Phosphorylation of large tumour antigen by cdc2 stimulates SV40 DNA replication

Nature ◽  
1989 ◽  
Vol 341 (6242) ◽  
pp. 503-507 ◽  
Author(s):  
Duncan McVey ◽  
Leonardo Brizuela ◽  
Ian Mohr ◽  
Daniel R. Marshak ◽  
Yasha Gluzman ◽  
...  
Keyword(s):  
Dna Replication ◽  
Tumour Antigen ◽  
Large Tumour ◽  
Sv40 Dna

Initiation of SV40 DNA replication in vivo: Location and structure of 5′ ends of DNA synthesized in the ori region

Cell ◽  
1982 ◽  
Vol 28 (4) ◽  
pp. 767-779 ◽  
Author(s):  
Ronald T. Hay ◽  
Melvin L. Depamphilis
Keyword(s):  
Dna Replication ◽  
Sv40 Dna

Replication of cloned DNA containing the Alu family sequence during cell extract-promoting simian virus 40 DNA synthesis

1984 ◽  
Vol 4 (8) ◽  
pp. 1476-1482
Author(s):  
H Ariga
Keyword(s):  
Dna Replication ◽  
Dna Synthesis ◽  
Rna Polymerase Iii ◽  
Simian Virus 40 ◽  
Cell Extract ◽  
Simian Virus ◽  
T Antigen ◽  
Sv40 T Antigen ◽  
Sv40 Dna

The replicating activity of several cloned DNAs containing putative origin sequences was examined in a cell-free extract that absolutely depends on simian virus 40 (SV40) T antigen promoting initiation of SV40 DNA replication in vitro. Of the three DNAs containing the human Alu family sequence (BLUR8), the origin of (Saccharomyces cerevisiae plasmid 2 micron DNA (pJD29), and the yeast autonomous replicating sequence (YRp7), only BLUR8 was active as a template. Replication in a reaction mixture with BLUR8 as a template was semiconservative and not primed by a putative RNA polymerase III transcript synthesized on the Alu family sequence in vitro. Pulse-chase experiments showed that the small-sized DNA produced in a short-term incubation was converted to full-length closed circular and open circular DNAs in alkaline sucrose gradients. DNA synthesis in extracts began in a region of the Alu family sequence and was inhibited 80% by the addition of anti-T serum. Furthermore, partially purified T antigen bound the Alu family sequence in BLUR8 by the DNA-binding immunoassay. These results suggest that SV40 T antigen recognizes the Alu family sequence, similar to the origin sequence of SV40 DNA, and initiates semiconservative DNA replication in vitro.

scholarly journals Structures of large T antigen at the origin of SV40 DNA replication by atomic force microscopy

1994 ◽  
Vol 66 (2) ◽  
pp. 293-298 ◽  
Author(s):  
I.A. Mastrangelo ◽  
M. Bezanilla ◽  
P.K. Hansma ◽  
P.V. Hough ◽  
H.G. Hansma
Keyword(s):  
Atomic Force Microscopy ◽  
Dna Replication ◽  
T Antigen ◽  
Large T Antigen ◽  
Force Microscopy ◽  
Atomic Force ◽  
Sv40 Dna

In vitro replication of DNA containing either the SV40 or the polyoma origin

1987 ◽  
Vol 317 (1187) ◽  
pp. 439-453 ◽  
Keyword(s):  
Dna Replication ◽  
Dna Polymerase ◽  
Hela Cells ◽  
Dna Binding Protein ◽  
T Antigen ◽  
Sv40 T Antigen ◽  
Sv40 Origin ◽  
Sv40 Dna ◽  
Primase Complex

The replication of DNA containing either the polyoma or SV40 origin has been done in vitro . Each system requires its cognate large-tumour antigen (T antigen) and extracts from cells that support its replication in vivo . The host-cell source of DNA polymerase α - primase complex plays an important role in discriminating between polyoma T antigen and SV40 T antigen-dependent replication of their homologous DNA. The SV40 origin- and T antigen-dependent DNA replication has been reconstituted in vitro with purified protein components isolated from HeLa cells. In addition to SV40 T antigen, HeLa DNA polymerase α - primase complex, eukaryotic topoisomerase I and a single-strand DNA binding protein from HeLa cells are required. The latter activity, isolated solely by its ability to support SV40 DNA replication, sediments and copurifies with two major protein species of 72 and 76 kDa. Although crude fractions yielded closed circular monomer products, the purified system does not. However, the addition of crude fractions to the purified system resulted in the formation of replicative form I (RFI) products. We have separated the replication reaction with purified components into multiple steps. In an early step, T antigen in conjunction with a eukaryotic topoisomerase (or DNA gyrase) and a DNA binding protein, catalyses the conversion of a circular duplex DNA molecule containing the SV40 origin to a highly underwound covalently closed circle. This reaction requires the action of a helicase activity and the SV40 T antigen preparation contains such an activity. The T antigen associated ability to unwind DNA copurified with other activities intrinsic to T antigen (ability to support replication of SV40 DNA containing the SV40 origin, poly dT-stimulated ATPase activity and DNA helicase).

Identification of replication factor C from Saccharomyces cerevisiae: a component of the leading-strand DNA replication complex

1992 ◽  
Vol 12 (1) ◽  
pp. 155-163 ◽  
Author(s):  
K Fien ◽  
B Stillman
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Replication ◽  
Dna Polymerase ◽  
Replication Factor C ◽  
Dna Polymerase Delta ◽  
Replication Complex ◽  
Leading Strand ◽  
Factor C ◽  
Sv40 Dna

A number of proteins have been isolated from human cells on the basis of their ability to support DNA replication in vitro of the simian virus 40 (SV40) origin of DNA replication. One such protein, replication factor C (RFC), functions with the proliferating cell nuclear antigen (PCNA), replication protein A (RPA), and DNA polymerase delta to synthesize the leading strand at a replication fork. To determine whether these proteins perform similar roles during replication of DNA from origins in cellular chromosomes, we have begun to characterize functionally homologous proteins from the yeast Saccharomyces cerevisiae. RFC from S. cerevisiae was purified by its ability to stimulate yeast DNA polymerase delta on a primed single-stranded DNA template in the presence of yeast PCNA and RPA. Like its human-cell counterpart, RFC from S. cerevisiae (scRFC) has an associated DNA-activated ATPase activity as well as a primer-template, structure-specific DNA binding activity. By analogy with the phage T4 and SV40 DNA replication in vitro systems, the yeast RFC, PCNA, RPA, and DNA polymerase delta activities function together as a leading-strand DNA replication complex. Now that RFC from S. cerevisiae has been purified, all seven cellular factors previously shown to be required for SV40 DNA replication in vitro have been identified in S. cerevisiae.

Bovine RP-A Functions in SV40 DNA Replication in vitro, but Bovine Polymerase α-Primase Inhibits Replication Competitively

1992 ◽  
pp. 385-397 ◽  
Author(s):  
Christine Schneider ◽  
Dorothea von Winkler ◽  
Irene Dornreiter ◽  
Heinz-Peter Nasheuer ◽  
Ilka Gilbert ◽  
...  
Keyword(s):  
Dna Replication ◽  
Sv40 Dna

SV40 DNA Replication In Vitro

1989 ◽  
pp. 437-448
Author(s):  
Mark K. Kenny ◽  
Ann D. Kwong ◽  
Suk-Hee Lee ◽  
Takashi Matsumoto ◽  
Yeon Soo Seo ◽  
...  
Keyword(s):  
Dna Replication ◽  
Sv40 Dna

scholarly journals Activation of SV40 DNA replication in vitro by cellular protein phosphatase 2A.

1989 ◽  
Vol 8 (12) ◽  
pp. 3891-3898 ◽  
Author(s):  
D.M. Virshup ◽  
M.G. Kauffman ◽  
T.J. Kelly
Keyword(s):  
Dna Replication ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Cellular Protein ◽  
Phosphatase 2A ◽  
Sv40 Dna
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