Multimerization and transcriptional activation of the phosphoprotein (P) of vesicular stomatitis virus by casein kinase-II.

Gao, Yuan; Lenard, John

doi:10.1002/j.1460-2075.1995.tb07107.x

Cited by 97 publications

(140 citation statements)

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“…Studies on a number of viruses ranging from rhabdovirus to paramyxovirus report a different oligomeric status of P protein including dimer, trimer, and tetramer (9,(11)(12)(13)17). By gel filtration, DLS, and chemical cross-linking analyses, we have shown that the RPV P protein exists as a tetramer in solution, and the tetramerization is through the coiled coil region of the C-terminal domain.…”

Section: Discussionmentioning

confidence: 85%

“…Although earlier work on P proteins from SeV, NDV, and MuV suggested that P could be a trimer, recent structural analyses using various biophysical methods and crystallographic study reveal that SeV P is a tetramer (13,21). Though VSV P protein is reported to be a trimer, it is also suggested to form a tetramer (9,11). It might be noted that the study with rabies virus (a rhabdovirus) P also does not exclude the possibility of tetramer formation (12).…”

Section: Discussionmentioning

confidence: 99%

“…While the P protein of VSV and chandipura virus (ChP) (rhabdovirus) require phosphorylation to facilitate its oligomerization, P proteins from paramyxoviruses such as SeV, NDV, MuV, and MV have been shown to oligomerize independent of phosphorylation (7,9,17,19). Moreover unlike VSV P and ChV P, rabies virus (another rhabdovirus) P protein can form an oligomer in the absence of any phosphorylation (12).…”

Section: Discussionmentioning

confidence: 99%

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Phosphoprotein of the Rinderpest Virus Forms a Tetramer through a Coiled Coil Region Important for Biological Function

Rahaman

Srinivasan

Shamala

et al. 2004

Journal of Biological Chemistry

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Phosphoprotein (P) of negative sense RNA viruses functions as a transcriptional transactivator of the viral polymerase (L). We report here the characterization of oligomeric P protein of rinderpest virus (RPV) and provide a structural basis for its multimerization. By size exclusion chromatography and dynamic light scattering analyses we show that bacterially expressed P protein exists as an oligomer, thus excluding the role of phosphorylation in P protein oligomerization. Gel filtration analyses of various parts of the P protein, also expressed in Escherichia coli, revealed that the predicted coiled coil region in the C-terminal domain is responsible for P protein oligomerization. Dynamic light scattering analysis confirmed the oligomeric nature of the coiled coil region of P. Chemical cross-linking analysis suggested that the C-terminal coiled coil region exists as a tetramer. The tetramer is formed by coiled coil interaction as shown by circular dichroism spectral analysis. Based on sequence homology, we propose a three-dimensional structure of the multimerization domain of RPV P using the crystal structure for multimerization domain of sendai virus (SeV) P as a template. Four-stranded coiled coil structure of the model is stabilized by a series of interactions predominantly between short nonpolar side chains emerging from different strands. In an in vivo replication/transcription system using a synthetic minigenome of RPV, we show that multimerization is essential for P protein function(s), and the multimerization domain is highly conserved between two morbilliviruses namely RPV and peste de petits ruminants virus. These results are discussed in the context of biological functions of P protein among various negative-stranded RNA viruses.

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Section: Discussionmentioning

confidence: 85%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Phosphoprotein of the Rinderpest Virus Forms a Tetramer through a Coiled Coil Region Important for Biological Function

Rahaman

Srinivasan

Shamala

et al. 2004

Journal of Biological Chemistry

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“…It is assumed that oligomer formation facilitates movement of P (and most likely of the complete polymerase complex) on the RNA template, thereby maintaining polymerase processivity (4). A requirement of P oligomers for viral RNA synthesis was also described for P proteins of other viruses of the order Mononegavirales, including vesicular stomatitis virus (10,11) and human parainfluenza virus type 3 (12). For the P protein of Sendai virus and human parainfluenza virus type 3, a defined coiled coil region is sufficient for oligomer formation (8,13).…”

mentioning

confidence: 93%

“…For the P protein of Sendai virus and human parainfluenza virus type 3, a defined coiled coil region is sufficient for oligomer formation (8,13). By contrast, vesicular stomatitis virus P oligomerization only occurs prior to phosphorylation of two amino acid residues in the N-terminal acidic region (11). Interestingly, phosphorylation-negative vesicular stomatitis virus P mutants are fully active in replication but defective in transcription (14), suggesting that the viral transcriptase and replicase are two distinct entities with different subunit composition.…”

mentioning

confidence: 99%

Overlap of Interaction Domains Indicates a Central Role of the P Protein in Assembly and Regulation of the Borna Disease Virus Polymerase Complex

Schneider

Blechschmidt

Schwemmle

et al. 2004

Journal of Biological Chemistry

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The 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.The active transcription and replication complex of non-segmented negative strand RNA viruses, termed ribonucleoprotein complex (1), consists of the viral polymerase (L), 1 the phosphoprotein (P), the nucleoprotein (N), and the viral RNA (2). P is a co-transcriptional factor of L, whereas N encapsidates the viral genome to form N⅐RNA complexes (3). For Sendai virus, a prototype paramyxovirus, it was shown that P acts as a scaffold protein, which brings L into close proximity to the N⅐RNA complex (4), thus allowing RNA synthesis. In the absence of P, the N⅐RNA complexes are not recognized by L (5). The viral P protein exerts this scaffolding function by employing independent binding sites for L and the N⅐RNA complex (6). P of Sendai virus contains an additional but distinct binding domain for free N (not bound to viral RNA) (7) and a domain required for multimer formation (8, 9). Complex formation between P and free N prevents aggregation of N (7). Oligomerization is an essential prerequisite for Sendai virus P function in viral transcription and replication (4). The precise function of oligomeric P is unclear. It is assumed that oligomer formation facilitates movement of P (and most likely of the complete polymerase complex) on the RNA template, thereby maintaining polymerase processivity (4). A requirement of P oligomers for viral RNA synthesis was also described for P proteins of other viruses of the order Mononegavirales, including vesicular stomatitis virus (10, 11) and human parainfluenza virus type 3 (12). For the P protein of Sendai virus and human parainfluenza virus type 3, a de...

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Protein kinase CK2 and its role in cellular proliferation, development and pathology

Guerra¹,

Issinger²

1999

Electrophoresis

367

236

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Multimerization and transcriptional activation of the phosphoprotein (P) of vesicular stomatitis virus by casein kinase-II.

Cited by 97 publications

References 31 publications

Phosphoprotein of the Rinderpest Virus Forms a Tetramer through a Coiled Coil Region Important for Biological Function

Phosphoprotein of the Rinderpest Virus Forms a Tetramer through a Coiled Coil Region Important for Biological Function

Overlap of Interaction Domains Indicates a Central Role of the P Protein in Assembly and Regulation of the Borna Disease Virus Polymerase Complex

Protein kinase CK2 and its role in cellular proliferation, development and pathology

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