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Basic Characteristics of Mutations
|
|
Mutation Site
|
K207A |
|
Mutation Site Sentence
|
The BZLF1 mutant proteins all gave similar levels of protein expression (measured by the incorporation of [35S]Met) when translated in vitro in reticulocyte lysate (Fig. 2A), and all apart from K207A/L214A gave a measureable shift in the EMSA (Fig. 2B). |
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Mutation Level
|
Amino acid level |
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Mutation Type
|
Nonsynonymous substitution |
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Gene/Protein/Region
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BZLF1 |
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Standardized Encoding Gene
|
BZLF1
|
|
Genotype/Subtype
|
- |
|
Viral Reference
|
-
|
|
Functional Impact and Mechanisms
|
|
Disease
|
-
|
|
Immune
|
- |
|
Target Gene
|
-
|
|
Clinical and Epidemiological Correlations
|
|
Clinical Information
|
- |
|
Treatment
|
- |
|
Location
|
- |
|
Literature Information
|
|
PMID
|
19144704
|
|
Title
|
Interaction of Epstein-Barr virus BZLF1 C-terminal tail structure and core zipper is required for DNA replication but not for promoter transactivation
|
|
Author
|
McDonald CM,Petosa C,Farrell PJ
|
|
Journal
|
Journal of virology
|
|
Journal Info
|
2009 Apr;83(7):3397-401
|
|
Abstract
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The Epstein-Barr virus (EBV) protein BZLF1 contains a bZIP DNA binding domain in which C-terminal tail residues fold back against a zipper region that forms a coiled coil and mediates dimerization. Point mutagenesis in the zipper region reveals the importance of individual residues within the (208)SSENDRLR(215) sequence that is conserved in C/EBP for transactivation and EBV DNA replication. The restoration of BZLF1 DNA replication activity by the complementation of two deleterious mutations (S208E and D236K) indicates that the interaction of the C-terminal tail and the core zipper is required for DNA replication, identifying a functional role for this structural feature unique to BZLF1.
|
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Sequence Data
|
-
|