Abstract
LEF-3 and P143 are two of six proteins encoded by the Autographa californica multinucleocapsid nucleopolyhedrovirus genome which are required for DNA replication in transient replication assays. LEF-3 has the properties of an ssDNA-binding protein and P143 exhibits amino acid sequence homology to helicases. In this report, the interaction of LEF-3 and P143 was studied by yeast two-hybrid and immunoaffinity analyses. Using the yeast two-hybrid system, the interaction domain of LEF-3 (385 aa) was mapped to amino acids between positions 1 and 165. Deletion analysis of P143 failed to reveal an interaction domain, suggesting that there were either multiple interaction domains or that the deletions disrupted the secondary structures required for the interaction between LEF-3 and P143.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Base Sequence
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DNA Helicases / chemistry
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DNA Helicases / genetics
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DNA Helicases / metabolism*
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DNA Primers / genetics
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DNA Replication
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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Escherichia coli / genetics
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Immediate-Early Proteins / chemistry
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Immediate-Early Proteins / genetics
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Immediate-Early Proteins / metabolism*
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Nucleopolyhedroviruses / genetics
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Nucleopolyhedroviruses / metabolism*
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Protein Structure, Secondary
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Saccharomyces cerevisiae / genetics
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Sequence Deletion
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Trans-Activators / chemistry
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Trans-Activators / genetics
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Trans-Activators / metabolism*
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Viral Proteins / chemistry
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Viral Proteins / genetics
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Viral Proteins / metabolism*
Substances
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DNA Primers
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DNA-Binding Proteins
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Immediate-Early Proteins
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Trans-Activators
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Viral Proteins
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late expression factor 3, baculovirus
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IE2 protein, polyhedrosis virus
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DNA Helicases