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Literature DB >> 2536153

Sequence independent duplex DNA opening reaction catalysed by SV40 large tumor antigen.

Abstract

Simian virus 40 (SV40) large tumor antigen (T antigen) is mainly localized in the nucleus where it exhibits two biochemical properties: DNA binding and helicase activity. Both activities are necessary for viral DNA replication and may also enable T antigen to modulate cellular growth. Here we present biochemical and electron microscopic evidence that the helicase activity can start at internal sites of fully double-stranded DNA molecules not containing the SV40 origin or replication. Using T antigen specific monoclonal antibodies, this unwinding reaction can be biochemically divided in an initiation (duplex opening) and a propagation step. The duplex opening reaction (as well as the propagation step) does not depend on a specific DNA sequence or secondary structure. In addition, we have found that T antigen forms an ATP dependent nucleoprotein complex at double-stranded DNA, which may be an essential step for the sequence independent duplex DNA opening reaction.

Entities: Disease Species

Mesh：

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Year: 1989 PMID： 2536153 PMCID： PMC331537 DOI： 10.1093/nar/17.1.93

Source DB: PubMed Journal: Nucleic Acids Res ISSN： 0305-1048 Impact factor: 16.971

34 in total

1. Simian virus 40 large tumor antigen requires three core replication origin domains for DNA unwinding and replication in vitro.

Authors: F B Dean; J A Borowiec; Y Ishimi; S Deb; P Tegtmeyer; J Hurwitz
Journal: Proc Natl Acad Sci U S A Date: 1987-12 Impact factor: 11.205

2. ATP-dependent formation of a specialized nucleoprotein structure by simian virus 40 (SV40) large tumor antigen at the SV40 replication origin.

Authors: F B Dean; M Dodson; H Echols; J Hurwitz
Journal: Proc Natl Acad Sci U S A Date: 1987-12 Impact factor: 11.205

3. The unwinding of duplex regions in DNA by the simian virus 40 large tumor antigen-associated DNA helicase activity.

Authors: G S Goetz; F B Dean; J Hurwitz; S W Matson
Journal: J Biol Chem Date: 1988-01-05 Impact factor: 5.157

4. A routine method for protein-free spreading of double- and single-stranded nucleic acid molecules.

Authors: H J Vollenweider; J M Sogo; T Koller
Journal: Proc Natl Acad Sci U S A Date: 1975-01 Impact factor: 11.205

5. Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.

Authors: M Wiekowski; M W Schwarz; H Stahl
Journal: J Biol Chem Date: 1988-01-05 Impact factor: 5.157

Review 6. The simian virus 40 large tumor antigen.

Authors: H Stahl; R Knippers
Journal: Biochim Biophys Acta Date: 1987-10-09

7. Unwinding of duplex DNA from the SV40 origin of replication by T antigen.

Authors: M Dodson; F B Dean; P Bullock; H Echols; J Hurwitz
Journal: Science Date: 1987-11-13 Impact factor: 47.728

8. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors: U K Laemmli
Journal: Nature Date: 1970-08-15 Impact factor: 49.962

9. Escherichia coli DNA helicase I catalyzes a unidirectional and highly processive unwinding reaction.

Authors: E E Lahue; S W Matson
Journal: J Biol Chem Date: 1988-03-05 Impact factor: 5.157

10. The ease of DNA unwinding as a determinant of initiation at yeast replication origins.

Authors: R M Umek; D Kowalski
Journal: Cell Date: 1988-02-26 Impact factor: 41.582

14 in total

1. Nonspecific DNA binding activity of simian virus 40 large T antigen: evidence for the cooperation of two regions for full activity.

Authors: H J Lin; R H Upson; D T Simmons
Journal: J Virol Date: 1992-09 Impact factor: 5.103

10. Simian virus 40 T-antigen DNA helicase is a hexamer which forms a binary complex during bidirectional unwinding from the viral origin of DNA replication.

Authors: R Wessel; J Schweizer; H Stahl
Journal: J Virol Date: 1992-02 Impact factor: 5.103

Sequence independent duplex DNA opening reaction catalysed by SV40 large tumor antigen.

1. Simian virus 40 large tumor antigen requires three core replication origin domains for DNA unwinding and replication in vitro.

2. ATP-dependent formation of a specialized nucleoprotein structure by simian virus 40 (SV40) large tumor antigen at the SV40 replication origin.

3. The unwinding of duplex regions in DNA by the simian virus 40 large tumor antigen-associated DNA helicase activity.

4. A routine method for protein-free spreading of double- and single-stranded nucleic acid molecules.

5. Simian virus 40 large T antigen DNA helicase. Characterization of the ATPase-dependent DNA unwinding activity and its substrate requirements.

Review 6. The simian virus 40 large tumor antigen.

7. Unwinding of duplex DNA from the SV40 origin of replication by T antigen.

8. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

9. Escherichia coli DNA helicase I catalyzes a unidirectional and highly processive unwinding reaction.

10. The ease of DNA unwinding as a determinant of initiation at yeast replication origins.

1. Nonspecific DNA binding activity of simian virus 40 large T antigen: evidence for the cooperation of two regions for full activity.

2. The N-terminal side of the origin-binding domain of simian virus 40 large T antigen is involved in A/T untwisting.

3. ATP-dependent minor groove recognition of TA base pairs is required for template melting by the E1 initiator protein.

4. Thermally inactivated simian virus 40 tsA58 mutant T antigen cannot initiate viral DNA replication in vitro.

5. Mapping of helicase and helicase substrate-binding domains on simian virus 40 large T antigen.

6. The initiator protein E1 binds to the bovine papillomavirus origin of replication as a trimeric ring-like structure.

7. Preformed hexamers of SV40 T antigen are active in RNA and origin-DNA unwinding.

8. Specific mutation of a regulatory site within the ATP-binding region of simian virus 40 large T antigen.

9. Two conditional tsA mutant simian virus 40 T antigens display marked differences in thermal inactivation.

10. Simian virus 40 T-antigen DNA helicase is a hexamer which forms a binary complex during bidirectional unwinding from the viral origin of DNA replication.