NDLI: Nonspecific Double-Stranded DNA Binding Activity of Simian Virus 40 Large T Antigen Is Involved in Melting and Unwinding of the Origin

Content Provider	PubMed Central
Author	Jiao, Junfang Simmons, Daniel T.
Copyright Year	2003
Abstract	Helicase activity is required for T antigen to unwind the simian virus 40 origin. We previously mapped this activity to residues 131 and 616. In this study, we generated a series of mutants with single-point substitutions in the helicase domain to discover other potential activities required for helicase function. A number of DNA unwinding-defective mutants were generated. Four of these mutants (456RA, 460ED, 462GA, and 499DA) were normal in their ability to hydrolyze ATP and were capable of associating into double hexamers in the presence of origin DNA. Furthermore, they possessed normal ability to bind to single-stranded DNA. However, they were severely impaired in unwinding origin-containing DNA fragments and in carrying out a helicase reaction with an M13 partial duplex DNA substrate. Interestingly, these mutants retained some ability to perform a helicase reaction with artificial replication forks, indicating that their intrinsic helicase activity was functional. Intriguingly, these mutants had almost completely lost their ability to bind to double-stranded DNA nonspecifically. The mutants also failed to melt the early palindrome region of the origin. Taken together, these results indicate that the mutations have destroyed a novel activity required for unwinding of the origin. This activity depends on the ability to bind to DNA nonspecifically, and in its absence, T antigen is unable to structurally distort and subsequently unwind the origin.
Related Links	http://dx.doi.org/10.1128/JVI.77.23.12720-12728.2003
Starting Page	12720
File Format	PDF
ISSN	10985514
e-ISSN	10985514
Journal	Journal of Virology
Issue Number	23
Volume Number	77
Language	English
Publisher	American Society for Microbiology
Publisher Date	2003-12-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Virology Immunology Microbiology Insect Science

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The Origin DNA-Binding and Single-Stranded DNA-Binding Domains of Simian Virus 40 Large T Antigen Are Distinct

Oligomerization and origin DNA-binding activity of simian virus 40 large T antigen.

Discrete regions of simian virus 40 large T antigen are required for nonspecific and viral origin-specific DNA binding.

Analyses of the Interaction between the Origin Binding Domain from Simian Virus 40 T Antigen and Single-Stranded DNA Provide Insights into DNA Unwinding and Initiation of DNA Replication▿

Simian virus 40 origin DNA-binding domain on large T antigen.

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

Role of Single-Stranded DNA Binding Activity of T Antigen in Simian Virus 40 DNA Replication

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

Four major sequence elements of simian virus 40 large T antigen coordinate its specific and nonspecific DNA binding.

Nonspecific Double-Stranded DNA Binding Activity of Simian Virus 40 Large T Antigen Is Involved in Melting and Unwinding of the Origin

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The Origin DNA-Binding and Single-Stranded DNA-Binding Domains of Simian Virus 40 Large T Antigen Are Distinct

Oligomerization and origin DNA-binding activity of simian virus 40 large T antigen.

Discrete regions of simian virus 40 large T antigen are required for nonspecific and viral origin-specific DNA binding.

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Nonspecific Double-Stranded DNA Binding Activity of Simian Virus 40 Large T Antigen Is Involved in Melting and Unwinding of the Origin