Human cytomegalovirus pp65 lower matrix phosphoprotein harbours two transplantable nuclear localization signals
| Autor: | Elena Percivalle, Lavinia Simoncini, G. Gerna, M G Revello, Gabriele Milanesi, Andrea Gallina |
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| Rok vydání: | 1996 |
| Předmět: |
Chloramphenicol O-Acetyltransferase
viruses Molecular Sequence Data Cytomegalovirus Spodoptera Biology Transfection Polymerase Chain Reaction 3T3 cells Cell Line Viral Matrix Proteins Chloramphenicol acetyltransferase Mice Open Reading Frames Virology medicine Animals Humans Point Mutation Amino Acid Sequence Cloning Molecular Lung Sequence Deletion Sequence Tagged Sites Cell Nucleus Base Sequence Antibodies Monoclonal virus diseases 3T3 Cells Phosphoproteins Molecular biology Recombinant Proteins Cell nucleus medicine.anatomical_structure Phosphoprotein Mutagenesis Site-Directed Phosphorylation Casein kinase 2 Nuclear localization sequence Signal Transduction |
| Zdroj: | Journal of General Virology. 77:1151-1157 |
| ISSN: | 1465-2099 0022-1317 |
| Popis: | Human cytomegalovirus phosphoprotein pp65 is targeted to the cell nucleus immediately after infection. Deletion and point mutation analysis of the pp65 gene expressed in insect cells showed that two hydrophilic regions (HP1 and HP2) within the pp65 C-terminal 40% each harboured an independent nuclear localization signal (NLS); strong association to the nuclear stroma also requires the N-terminal domain. Either region, when fused to chloramphenicol acetyltransferase, localized the reporter protein to the nucleus in insect cells as well as in NIH 3T3 cells and human lung fibroblasts. In addition, HP1 was found to be the target of pp65 Ser/Thr phosphorylation in insect cells and a prokaryotically expressed HP1 was actively phosphorylated in vitro by casein kinase II, for which two site clusters map in HP1. These findings indicate that pp65 includes two NLSs, one of which has the potential to be modulated by phosphorylation. |
| Databáze: | OpenAIRE |
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