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A functional study of nucleocytoplasmic transport signals of the EhNCABP166 protein from Entamoeba histolytica
- Source :
- Parasitology. 139(13)
- Publication Year :
- 2012
-
Abstract
- SUMMARYEhNCABP166 is an Entamoeba histolytica actin-binding protein that localizes to the nucleus and cytoplasm. Bioinformatic analysis of the EhNCABP166 amino acid sequence shows the presence of 3 bipartite nuclear localization signals (NLS) and a nuclear export signal (NES). The present study aimed to investigate the functionality of these signals in 3 ways. First, we fused each potential NLS to a cytoplasmic domain of ehFLN to determine whether the localization of this domain could be altered by the presence of the NLSs. Furthermore, the localization of each domain of EhNCABP166 was determined. Similarly, we generated mutations in the first block of bipartite signals from the domains that contained these signals. Additionally, we added an NES to 2 constructs that were then evaluated. We confirmed the intranuclear localization of EhNCABP166 using transmission electron microscopy. Fusion of each NLS resulted in shuttling of the cytoplasmic domain to the nucleus. With the exception of 2 domains, all of the evaluated domains localized within the nucleus. A mutation in the first block of bipartite signals affected the localization of the domains containing an NLS. The addition of an NES shifted the localization of these domains to the cytoplasm. The results presented here establish EhNCABP166 as a protein containing functional nuclear localization signals and a nuclear export signal.
- Subjects :
- Cytoplasm
Nuclear Localization Signals
Active Transport, Cell Nucleus
Protozoan Proteins
Importin
Biology
Microscopy, Electron, Transmission
medicine
NLS
Trophozoites
Nuclear protein
Nuclear export signal
Cell Nucleus
Nuclear Export Signals
Entamoeba histolytica
Cell biology
Cell nucleus
Infectious Diseases
medicine.anatomical_structure
Biochemistry
Mutation
Animal Science and Zoology
Parasitology
Nucleus
Nuclear localization sequence
Subjects
Details
- ISSN :
- 14698161
- Volume :
- 139
- Issue :
- 13
- Database :
- OpenAIRE
- Journal :
- Parasitology
- Accession number :
- edsair.doi.dedup.....556e6be4fd7738c59f88739ced829807