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Biochemical and Biophysical Properties of a Putative Hub Protein Expressed by Vaccinia Virus
- Source :
- Journal of Biological Chemistry. 288:11470-11481
- Publication Year :
- 2013
- Publisher :
- Elsevier BV, 2013.
-
Abstract
- H5 is a constitutively expressed, phosphorylated vaccinia virus protein that has been implicated in viral DNA replication, post-replicative gene expression, and virus assembly. For the purpose of understanding the role of H5 in vaccinia biology, we have characterized its biochemical and biophysical properties. Previously, we have demonstrated that H5 is associated with an endoribonucleolytic activity. In this study, we have shown that this cleavage results in a 3'-OH end suitable for polyadenylation of the nascent transcript, corroborating a role for H5 in vaccinia transcription termination. Furthermore, we have shown that H5 is intrinsically disordered, with an elongated rod-shaped structure that preferentially binds double-stranded nucleic acids in a sequence nonspecific manner. The dynamic phosphorylation status of H5 influences this structure and has implications for the role of H5 in multiple processes during virus replication.
- Subjects :
- DNA Replication
Polyadenylation
viruses
Vaccinia virus
RNA-binding protein
macromolecular substances
Biology
Virus Replication
Microbiology
Biochemistry
DNA-binding protein
Virus
Viral Proteins
chemistry.chemical_compound
Protein structure
Endoribonucleases
Vaccinia
Humans
Phosphorylation
Molecular Biology
musculoskeletal, neural, and ocular physiology
DNA replication
Cell Biology
Molecular biology
Protein Structure, Tertiary
Cell biology
nervous system
chemistry
Viral replication
Transcription Termination, Genetic
DNA, Viral
HeLa Cells
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 288
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi.dedup.....605ded2b6d943bb25bb83d04e5443f59