A PY-nuclear localization signal is required for nuclear accumulation of HCMV UL79 protein
- PMID: 22628116
- DOI: 10.1007/s00430-012-0243-4
A PY-nuclear localization signal is required for nuclear accumulation of HCMV UL79 protein
Abstract
Human cytomegalovirus UL79 protein is recently reported to be required for transcription or efficient accumulation of late viral mRNAs during viral infection. An absolute nuclear distribution of UL79 proteins has been observed with immunofluorescence assay, both during the infection of Flag-tagged UL79 recombinant virus and in the HFFs expressing HA-tagged UL79, with or without virus infection. However, little is known about the nuclear import mechanism of UL79 protein. Here, by utilizing living cells fluorescent microscopy, a predominant nuclear localization of UL79 protein in living cells was detected. Furthermore, the nuclear import of UL79 protein was demonstrated to be dependent on the transportin-1-mediated pathway. Finally, a hydrophobic PY-nuclear localization signal (PY-NLS) was delineated between the amino acids 66-92 of UL79 protein. Collectively, we provide evidence that a PY-NLS, firstly described in viral proteins, is responsible for the nuclear accumulation of UL79 protein.
Similar articles
-
An importin alpha/beta-recognized bipartite nuclear localization signal mediates targeting of the human herpes simplex virus type 1 DNA polymerase catalytic subunit pUL30 to the nucleus.Biochemistry. 2007 Aug 14;46(32):9155-63. doi: 10.1021/bi7002394. Epub 2007 Jul 20. Biochemistry. 2007. PMID: 17640102
-
A nonconventional nuclear localization signal within the UL84 protein of human cytomegalovirus mediates nuclear import via the importin alpha/beta pathway.J Virol. 2003 Mar;77(6):3734-48. doi: 10.1128/jvi.77.6.3734-3748.2003. J Virol. 2003. PMID: 12610148 Free PMC article.
-
The potential terminase subunit of human cytomegalovirus, pUL56, is translocated into the nucleus by its own nuclear localization signal and interacts with importin alpha.J Gen Virol. 2000 Sep;81(Pt 9):2231-2244. doi: 10.1099/0022-1317-81-9-2231. J Gen Virol. 2000. PMID: 10950981
-
Intermolecular masking of the HIV-1 Rev NLS by the cellular protein HIC: novel insights into the regulation of Rev nuclear import.Retrovirology. 2011 Mar 14;8:17. doi: 10.1186/1742-4690-8-17. Retrovirology. 2011. PMID: 21401918 Free PMC article.
-
Transportin-1 and Transportin-2: protein nuclear import and beyond.FEBS Lett. 2014 May 21;588(10):1857-68. doi: 10.1016/j.febslet.2014.04.023. Epub 2014 Apr 26. FEBS Lett. 2014. PMID: 24780099 Review.
Cited by
-
Better late than never: A unique strategy for late gene transcription in the beta- and gammaherpesviruses.Semin Cell Dev Biol. 2023 Sep 15;146:57-69. doi: 10.1016/j.semcdb.2022.12.001. Epub 2022 Dec 17. Semin Cell Dev Biol. 2023. PMID: 36535877 Free PMC article. Review.
-
The nuclear localization signal of CPSF6 governs post-nuclear import steps of HIV-1 infection.bioRxiv [Preprint]. 2024 Jun 24:2024.06.20.599834. doi: 10.1101/2024.06.20.599834. bioRxiv. 2024. Update in: PLoS Pathog. 2025 Jan 17;21(1):e1012354. doi: 10.1371/journal.ppat.1012354. PMID: 38979149 Free PMC article. Updated. Preprint.
-
Nuclear Effectors in Plant Pathogenic Fungi.Mycobiology. 2022 Sep 20;50(5):259-268. doi: 10.1080/12298093.2022.2118928. eCollection 2022. Mycobiology. 2022. PMID: 36404902 Free PMC article. Review.
-
Types of nuclear localization signals and mechanisms of protein import into the nucleus.Cell Commun Signal. 2021 May 22;19(1):60. doi: 10.1186/s12964-021-00741-y. Cell Commun Signal. 2021. PMID: 34022911 Free PMC article. Review.
-
Porcine Circovirus Type 2 Hijacks Host IPO5 to Sustain the Intracytoplasmic Stability of Its Capsid Protein.J Virol. 2022 Dec 14;96(23):e0152222. doi: 10.1128/jvi.01522-22. Epub 2022 Nov 21. J Virol. 2022. PMID: 36409110 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
