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The initiator protein E1 binds to the bovine papillomavirus origin of replication as a trimeric ring-like structure
被引:51
|作者:
Sedman, J
[1
]
Stenlund, A
[1
]
机构:
[1] COLD SPRING HARBOR LAB,COLD SPRING HARBOR,NY 11724
来源:
关键词:
DNA binding;
DNA replication;
initiator;
papillomavirus;
D O I:
10.1002/j.1460-2075.1996.tb00889.x
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
The replication initiator protein El binds to the origin of replication of bovine papillomavirus in several forms. El can bind to its recognition sequence as a monomer together with the viral transcription factor E2, or as a trimeric El complex. The trimerization of El is mediated by the sequence-specific binding of El to DNA, and results in an El complex that is linked topologically to the DNA because the three molecules of El form a ring-like structure that encircles the DNA. These results demonstrate that El utilizes unusual mechanisms for sequence-specific binding to DNA and for the generation of a structure that encircles the DNA. We believe that these forms of El bound to the origin of replication represent intermediates in a transition in the function of El, from a sequence-specific origin of replication recognition protein to a form of El that is competent for the initiation of viral DNA replication.
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页码:5085 / 5092
页数:8
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