Source:http://linkedlifedata.com/resource/pubmed/id/17394774
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2007-3-30
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pubmed:abstractText |
The p13 gene is uniquely present in Group II nucleopolyhedroviruses (NPVs) and some granuloviruses, but not in Group I NPVs. p13 gene was first described by our laboratory in Leucania separatamultiple nuclear polyhedrosis virus (Ls-p13) in 1995. However, the functions of Ls-P13 and of its homologues are unknown. When Ls-p13 was inserted into Autographa californica nucleopolyhedrovirus, a Group I NPV, polyhedra yield was inhibited. However, this inhibition was prevented when the leucine zipper-like domain of Ls-p13 was mutated. To determine the cause of this marked difference between Ls-P13 and leucine zipper mutated Ls-P13 (Ls-P13mL), oligomerization and secondary structure analyses were performed. High performance liquid chromatography and yeast two-hybrid assays indicated that neither Ls-P13 nor Ls-P13mL could form oligomers. Informatics and circular dichroism spectropolarimetry results further indicated marked secondary structural differences between Ls-P13 and Ls-P13mL. The LZLD of Ls-P13 has two extended heptad repeat units which form a hydrophobic surface, but it is short of a third hydrophobic heptad repeat unit for oligomerization. However, the mutated LZLD of Ls-P13mL lacks the above hydrophobic surface, and its secondary structure is markedly different. This difference in its secondary structure may explain why Ls-P13mL is unable to inhibit polyhedra yield.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1225-8687
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
40
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
232-8
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pubmed:meshHeading |
pubmed-meshheading:17394774-Amino Acid Sequence,
pubmed-meshheading:17394774-Animals,
pubmed-meshheading:17394774-Base Sequence,
pubmed-meshheading:17394774-Circular Dichroism,
pubmed-meshheading:17394774-Leucine Zippers,
pubmed-meshheading:17394774-Molecular Sequence Data,
pubmed-meshheading:17394774-Mutant Proteins,
pubmed-meshheading:17394774-Mutation,
pubmed-meshheading:17394774-Nucleopolyhedrovirus,
pubmed-meshheading:17394774-Protein Structure, Quaternary,
pubmed-meshheading:17394774-Protein Structure, Tertiary,
pubmed-meshheading:17394774-Spodoptera,
pubmed-meshheading:17394774-Two-Hybrid System Techniques,
pubmed-meshheading:17394774-Viral Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
Function and oligomerization study of the leucine zipper-like domain in P13 from Leucania separata multiple nuclear polyhedrosis virus.
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pubmed:affiliation |
Nanyang-Rothamsted Joint Laboratory for Insect Biology, Nanyang Normal University, Nanyang 473061, P. R. China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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