Warning: Undefined variable $zfal in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 525
Deprecated: str_replace(): Passing null to parameter #3 ($subject) of type array|string is deprecated in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 525
Warning: Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 530
Warning: Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 531
English Wikipedia
Nephropedia Template TP (
Twit Text
DeepDyve Pubget Overpricing |
lüll Overlap of interaction domains indicates a central role of the P protein in assembly and regulation of the Borna disease virus polymerase complex Schneider U; Blechschmidt K; Schwemmle M; Staeheli PJ Biol Chem 2004[Dec]; 279 (53): 55290-6The active polymerase complex of Borna disease virus is composed of the viral proteins N, P, and L. The viral X (negative regulatory factor) protein acts as a regulator of polymerase activity. Interactions of P with N and X were previously studied, but interactions with L were poorly defined. Using a mammalian two-hybrid system, we observed that L specifically interacts with P but not with N, X, or itself. Mapping of the L-binding domain in the P molecule revealed that it overlaps with two adjacent domains required for multimerization and interaction with N. Competition experiments showed that the interaction between L and P was inefficient when N was present, indicating that L may preferentially interact with free P in infected cells. Interestingly, a multimerization-defective P mutant maintained the ability to interact with L, N, and X but failed to support reporter gene expression from an artificial Borna disease virus minigenome. Furthermore, dominant negative effects on minigenome activity were only observed when P mutants with an intact multimerization domain were used, suggesting that P multimers, rather than monomers, exhibit biological activity. P mutants lacking functional interaction domains for L or N still formed complexes with these viral proteins when wild-type P was available as a bridging molecule, indicating that P multimers have the potential to act as scaffolds on which the RNA polymerase complex is assembled.|Binding, Competitive[MESH]|Borna disease virus/*enzymology[MESH]|Cell Line[MESH]|Chromatography, Gel[MESH]|DNA, Complementary/metabolism[MESH]|DNA-Directed RNA Polymerases/*chemistry[MESH]|Genes, Dominant[MESH]|Humans[MESH]|Mutation[MESH]|Phosphoproteins[MESH]|Plasmids/metabolism[MESH]|Point Mutation[MESH]|Protein Binding[MESH]|Protein Structure, Tertiary[MESH]|Two-Hybrid System Techniques[MESH]|Viral Proteins/*chemistry[MESH]|Viral Structural Proteins/*chemistry/physiology[MESH] |