Abstract:
:Viral initiators perform multiple functions in initiation of DNA replication including ori binding, melting, and unwinding, culminating in the formation of a double hexameric (DH) helicase. We have recapitulated the assembly of the papillomavirus E1 initiator DH helicase, providing the first description of how such a complex is formed. We have identified an intermediate, a double trimer (DT), which relies on two cooperating DNA binding activities to melt double-stranded DNA and generate a substrate for formation of the DH helicase. The formation of the DT is dependent on nucleotide binding, while formation of the DH also requires hydrolysable ATP. The DNA binding properties of the DT explain how E1, which binds to DNA as a dimer, can effect a transition to ring structures, such as the double hexamer. These results provide new insight into the intricate machinery that initiates DNA replication.
journal_name
Mol Celljournal_title
Molecular cellauthors
Schuck S,Stenlund Adoi
10.1016/j.molcel.2005.09.020subject
Has Abstractpub_date
2005-11-11 00:00:00pages
377-89issue
3eissn
1097-2765issn
1097-4164pii
S1097-2765(05)01641-2journal_volume
20pub_type
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