Post-translational processing of the tobacco etch virus 49-kDa small nuclear inclusion polyprotein: Identification of an internal cleavage site and delimitation of VPg and proteinase domains
| Autor: | T D Parks, W G Dougherty |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Reticulocytes
Polyproteins Molecular Sequence Data Restriction Mapping Picornaviridae Cleavage (embryo) Plant Viruses Viral Proteins Virology Complementary DNA Endopeptidases Animals Amino Acid Sequence Peptide sequence Gene chemistry.chemical_classification biology Tobacco etch virus Viral Core Proteins RNA biology.organism_classification Precipitin Tests Amino acid chemistry Biochemistry Electrophoresis Polyacrylamide Gel Rabbits Protein Processing Post-Translational |
| Zdroj: | Virology. 183:449-456 |
| ISSN: | 0042-6822 |
| DOI: | 10.1016/0042-6822(91)90974-g |
| Popis: | The 49,000-dalton (49-kDa) small nuclear inclusion (NI) protein of tobacco etch virus (TEV) has two distinct functions associated with it. An N-terminal segment is covalently attached to the genomic length RNA and likely involved in RNA replication, while the C-terminal half is associated with a proteolytic activity critical for genome expression. The junction delineating these two proteins has not been identified. We have analyzed naturally occurring cleavage products of TEV NI proteins and have identified a possible internal cleavage site between Glu and Gly residues at TEV 49-kDa NI protein amino acids 189-190. Similar 49-kDa-derived products are formed in cell-free translation studies in minor amounts upon the addition of excess amounts of NI protein. Cleavage of the 49-kDa (430 amino acids) protein is predicted to result in the formation of two products, 21-kDa (189 amino acids) and 27 kDa (241 amino acids) in size. Complementary DNA encoding the 27-kDa C-terminal portion of the 49-kDa protein gene was cloned into various DNA sequences. This allowed us to express the 27-kDa protein alone or as part of higher molecular weight polyproteins containing flanking TEV or foreign protein sequences. This 27-kDa amino acid sequence had a proteolytic activity similar to the 49-kDa-associated activity. |
| Databáze: | OpenAIRE |
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