Functional Analysis of Adenovirus Protein IX Identifies Domains Involved in Capsid Stability, Transcriptional Activity, and Nuclear Reorganization
Autor: | Manuel Rosa-Calatrava, Linda Grave, Claude Kedinger, Bruno Chatton, Francine Puvion-Dutilleul |
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Přispěvatelé: | Biotechnologie et signalisation cellulaire (BSC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut de recherche de l'Ecole de biotechnologie de Strasbourg (IREBS) |
Rok vydání: | 2001 |
Předmět: |
Transcription
Genetic Molecular Sequence Data Immunology Replication Mutagenesis (molecular biology technique) Adenovirus Protein Biology Microbiology Cell Line 03 medical and health sciences Transactivation Capsid Leucine Virology Humans [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence Gene 030304 developmental biology Cell Nucleus 0303 health sciences Alanine Functional analysis Adenoviruses Human 030302 biochemistry & molecular biology Promoter Protein Structure Tertiary 3. Good health Biochemistry Insect Science Trans-Activators Capsid Proteins Peptides |
Zdroj: | Journal of Virology Journal of Virology, American Society for Microbiology, 2020, 75 (15), pp.7131-7141. ⟨10.1128/JVI.75.15.7131-7141.2001⟩ |
ISSN: | 1098-5514 0022-538X |
Popis: | The product of adenovirus (Ad) type 5 gene IX (pIX) is known to actively participate in the stability of the viral icosahedron, acting as a capsid cement. We have previously demonstrated that pIX is also a transcriptional activator of several viral and cellular TATA-containing promoters, likely contributing to the transactivation of the Ad expression program. By extensive mutagenesis, we have now delineated the functional domains involved in each of the pIX properties: residues 22 to 26 of the highly conserved N-terminal domain are crucial for incorporation of the protein into the virion; specific residues of the C-terminal leucine repeat are responsible for pIX interactions with itself and possibly other proteins, a property that is critical for pIX transcriptional activity. We also show that pIX takes part in the virus-induced nuclear reorganization of late infected cells: the protein induces, most likely through self-assembly, the formation of specific nuclear structures which appear as dispersed nuclear globules by immunofluorescence staining and as clear amorphous spherical inclusions by electron microscopy. The integrity of the leucine repeat appears to be essential for the formation and nuclear retention of these inclusions. Together, our results demonstrate the multifunctional nature of pIX and provide new insights into Ad biology. |
Databáze: | OpenAIRE |
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