Three domains in the simian virus 40 core origin orchestrate the binding, melting, and DNA helicase activities of T antigen.

Abstract:

:The simian virus 40 (SV40) core origin of replication consists of three functional domains. The sequence 5'-CACTACTTCTGGAATAG-3' with an imperfect inverted repeat (underlined), a palindrome with four 5'-GAGGC-3' pentanucleotide repeats, and a 17-base-pair A + T-rich segment. We have been able to assign primary functions to each domain. Remarkably, SV40 large T antigen melted the inverted repeat domain in the complete absence of other origin sequences. Presumably, this protein-DNA interaction initiates a replication bubble that leads to daughter strand DNA synthesis. The pentanucleotide domain alone docked and arranged T antigen at the origin. The A + T-rich domain had no independent function, but, in the presence of the other two domains, allowed bound T antigen to extend the replication bubble. Thus, three domains of the origin coordinate the binding, melting, and DNA helicase activities of T antigen in an ordered sequence of events to initiate DNA replication.

journal_name

J Virol

journal_title

Journal of virology

authors

Parsons R,Anderson ME,Tegtmeyer P

doi

10.1128/JVI.64.2.509-518.1990

subject

Has Abstract

pub_date

1990-02-01 00:00:00

pages

509-18

issue

2

eissn

0022-538X

issn

1098-5514

journal_volume

64

pub_type

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