The Measles Virus Nucleocapsid Protein Tail Domain Is Dispensable for Viral Polymerase Recruitment and Activity
Paramyxovirus genomes are ribonucleoprotein (RNP) complexes consisting of nucleoprotein (N)-encapsidated viral RNA. Measles virus (MeV) N features an amino-terminal RNA-binding core and a 125-residue tail domain, of which only the last 75 residues are considered fully mobile on the nucleocapsid surf...
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Published in | The Journal of biological chemistry Vol. 288; no. 41; pp. 29943 - 29953 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
11.10.2013
American Society for Biochemistry and Molecular Biology |
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Abstract | Paramyxovirus genomes are ribonucleoprotein (RNP) complexes consisting of nucleoprotein (N)-encapsidated viral RNA. Measles virus (MeV) N features an amino-terminal RNA-binding core and a 125-residue tail domain, of which only the last 75 residues are considered fully mobile on the nucleocapsid surface. A molecular recognition element (MoRE) domain mediates binding of the viral phosphoprotein (P). This P N-tail interaction is considered instrumental for recruiting the polymerase complex to the template. We have engineered MeV N variants with tail truncations progressively eliminating the MoRE domain and upstream tail sections. Confirming previous reports, RNPs with N truncations lacking the carboxyl-terminal 43-residues harboring the MoRE domain cannot serve as polymerase template. Remarkably, further removal of all tail residues predicted to be surface-exposed significantly restores RNP bioactivity. Insertion of structurally dominant tags into the central N-tail section reduces bioactivity, but the negative regulatory effect of exposed N-tail stems is sequence-independent. Bioactive nucleocapsids lacking exposed N-tail sections are unable to sustain virus replication, because of weakened interaction of the advancing polymerase complex with the template. Deletion of the N-MoRE-binding domain in P abrogates polymerase recruitment to standard nucleocapsids, but polymerase activity is partially restored when N-tail truncated RNPs serve as template. Revising central elements of the current replication model, these data reveal that MeV polymerase is capable of productively docking directly to the nucleocapsid core. Dispensable for polymerase recruitment, N-MoRE binding to P-tail stabilizes the advancing polymerase-RNP complex and may rearrange unstructured central tail sections to facilitate polymerase access to the template.
Background: The carboxyl-terminal tail domain of the paramyxovirus nucleoprotein is considered instrumental for polymerase recruitment to the template.
Results: Truncated nucleoproteins reveal that the tail domain is dispensable for viral polymerase loading and activity.
Conclusion: The viral polymerase complex is capable of productively docking directly to the nucleocapsid core.
Significance: This finding alters the current paradigm of paramyxovirus polymerase recruitment. |
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AbstractList | Paramyxovirus genomes are ribonucleoprotein (RNP) complexes consisting of nucleoprotein (N)-encapsidated viral RNA. Measles virus (MeV) N features an amino-terminal RNA-binding core and a 125-residue tail domain, of which only the last 75 residues are considered fully mobile on the nucleocapsid surface. A molecular recognition element (MoRE) domain mediates binding of the viral phosphoprotein (P). This P N-tail interaction is considered instrumental for recruiting the polymerase complex to the template. We have engineered MeV N variants with tail truncations progressively eliminating the MoRE domain and upstream tail sections. Confirming previous reports, RNPs with N truncations lacking the carboxyl-terminal 43-residues harboring the MoRE domain cannot serve as polymerase template. Remarkably, further removal of all tail residues predicted to be surface-exposed significantly restores RNP bioactivity. Insertion of structurally dominant tags into the central N-tail section reduces bioactivity, but the negative regulatory effect of exposed N-tail stems is sequence-independent. Bioactive nucleocapsids lacking exposed N-tail sections are unable to sustain virus replication, because of weakened interaction of the advancing polymerase complex with the template. Deletion of the N-MoRE-binding domain in P abrogates polymerase recruitment to standard nucleocapsids, but polymerase activity is partially restored when N-tail truncated RNPs serve as template. Revising central elements of the current replication model, these data reveal that MeV polymerase is capable of productively docking directly to the nucleocapsid core. Dispensable for polymerase recruitment, N-MoRE binding to P-tail stabilizes the advancing polymerase-RNP complex and may rearrange unstructured central tail sections to facilitate polymerase access to the template.
Background: The carboxyl-terminal tail domain of the paramyxovirus nucleoprotein is considered instrumental for polymerase recruitment to the template.
Results: Truncated nucleoproteins reveal that the tail domain is dispensable for viral polymerase loading and activity.
Conclusion: The viral polymerase complex is capable of productively docking directly to the nucleocapsid core.
Significance: This finding alters the current paradigm of paramyxovirus polymerase recruitment. Background: The carboxyl-terminal tail domain of the paramyxovirus nucleoprotein is considered instrumental for polymerase recruitment to the template. Results: Truncated nucleoproteins reveal that the tail domain is dispensable for viral polymerase loading and activity. Conclusion: The viral polymerase complex is capable of productively docking directly to the nucleocapsid core. Significance: This finding alters the current paradigm of paramyxovirus polymerase recruitment. Paramyxovirus genomes are ribonucleoprotein (RNP) complexes consisting of nucleoprotein (N)-encapsidated viral RNA. Measles virus (MeV) N features an amino-terminal RNA-binding core and a 125-residue tail domain, of which only the last 75 residues are considered fully mobile on the nucleocapsid surface. A molecular recognition element (MoRE) domain mediates binding of the viral phosphoprotein (P). This P N-tail interaction is considered instrumental for recruiting the polymerase complex to the template. We have engineered MeV N variants with tail truncations progressively eliminating the MoRE domain and upstream tail sections. Confirming previous reports, RNPs with N truncations lacking the carboxyl-terminal 43-residues harboring the MoRE domain cannot serve as polymerase template. Remarkably, further removal of all tail residues predicted to be surface-exposed significantly restores RNP bioactivity. Insertion of structurally dominant tags into the central N-tail section reduces bioactivity, but the negative regulatory effect of exposed N-tail stems is sequence-independent. Bioactive nucleocapsids lacking exposed N-tail sections are unable to sustain virus replication, because of weakened interaction of the advancing polymerase complex with the template. Deletion of the N-MoRE-binding domain in P abrogates polymerase recruitment to standard nucleocapsids, but polymerase activity is partially restored when N-tail truncated RNPs serve as template. Revising central elements of the current replication model, these data reveal that MeV polymerase is capable of productively docking directly to the nucleocapsid core. Dispensable for polymerase recruitment, N-MoRE binding to P-tail stabilizes the advancing polymerase-RNP complex and may rearrange unstructured central tail sections to facilitate polymerase access to the template. Paramyxovirus genomes are ribonucleoprotein (RNP) complexes consisting of nucleoprotein (N)-encapsidated viral RNA. Measles virus (MeV) N features an amino-terminal RNA-binding core and a 125-residue tail domain, of which only the last 75 residues are considered fully mobile on the nucleocapsid surface. A molecular recognition element (MoRE) domain mediates binding of the viral phosphoprotein (P). This P N-tail interaction is considered instrumental for recruiting the polymerase complex to the template. We have engineered MeV N variants with tail truncations progressively eliminating the MoRE domain and upstream tail sections. Confirming previous reports, RNPs with N truncations lacking the carboxyl-terminal 43-residues harboring the MoRE domain cannot serve as polymerase template. Remarkably, further removal of all tail residues predicted to be surface-exposed significantly restores RNP bioactivity. Insertion of structurally dominant tags into the central N-tail section reduces bioactivity, but the negative regulatory effect of exposed N-tail stems is sequence-independent. Bioactive nucleocapsids lacking exposed N-tail sections are unable to sustain virus replication, because of weakened interaction of the advancing polymerase complex with the template. Deletion of the N-MoRE-binding domain in P abrogates polymerase recruitment to standard nucleocapsids, but polymerase activity is partially restored when N-tail truncated RNPs serve as template. Revising central elements of the current replication model, these data reveal that MeV polymerase is capable of productively docking directly to the nucleocapsid core. Dispensable for polymerase recruitment, N-MoRE binding to P-tail stabilizes the advancing polymerase-RNP complex and may rearrange unstructured central tail sections to facilitate polymerase access to the template. |
Author | Takeda, Makoto Krumm, Stefanie A. Plemper, Richard K. |
Author_xml | – sequence: 1 givenname: Stefanie A. surname: Krumm fullname: Krumm, Stefanie A. organization: From the Center for Inflammation, Immunity & Infection, Georgia State University, Atlanta, Georgia 30303 and – sequence: 2 givenname: Makoto surname: Takeda fullname: Takeda, Makoto organization: the Department of Virology III, National Institute of Infectious Diseases, Tokyo 208-0011, Musashimurayama, Japan – sequence: 3 givenname: Richard K. surname: Plemper fullname: Plemper, Richard K. email: rplemper@gsu.edu organization: From the Center for Inflammation, Immunity & Infection, Georgia State University, Atlanta, Georgia 30303 and |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24003217$$D View this record in MEDLINE/PubMed |
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Keywords | Virus Viral Replication Animal Viruses Microbiology Viral Polymerase |
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Snippet | Paramyxovirus genomes are ribonucleoprotein (RNP) complexes consisting of nucleoprotein (N)-encapsidated viral RNA. Measles virus (MeV) N features an... Background: The carboxyl-terminal tail domain of the paramyxovirus nucleoprotein is considered instrumental for polymerase recruitment to the template.... |
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SubjectTerms | Animal Viruses Animals Binding Sites - genetics Cell Line Chlorocebus aethiops Immunoblotting Measles virus - genetics Measles virus - metabolism Microbiology Models, Molecular Mutation Nucleocapsid Proteins Nucleoproteins - chemistry Nucleoproteins - genetics Nucleoproteins - metabolism Protein Binding Protein Structure, Tertiary Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - metabolism Ribonucleoproteins - chemistry Ribonucleoproteins - genetics Ribonucleoproteins - metabolism RNA-Dependent RNA Polymerase - chemistry RNA-Dependent RNA Polymerase - genetics RNA-Dependent RNA Polymerase - metabolism Vero Cells Viral Polymerase Viral Proteins - chemistry Viral Proteins - genetics Viral Proteins - metabolism Viral Replication Virus Virus Replication |
Title | The Measles Virus Nucleocapsid Protein Tail Domain Is Dispensable for Viral Polymerase Recruitment and Activity |
URI | https://dx.doi.org/10.1074/jbc.M113.503862 https://www.ncbi.nlm.nih.gov/pubmed/24003217 https://search.proquest.com/docview/1443405880 https://pubmed.ncbi.nlm.nih.gov/PMC3795292 |
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