Related Experiment Video
Updated: Jul 6, 2025

Methods to Investigate the Regulatory Role of Small RNAs and Ribosomal Occupancy of Plasmodium falciparum
Published on: December 4, 2015
Characterization of a nuclear transport factor 2-like domain-containing protein in Plasmodium berghei
Mamoru Niikura1, Toshiyuki Fukutomi2, Jiro Mitobe3
1Department of Infectious Diseases, Kyorin University School of Medicine, Tokyo, Japan. mniikura@ks.kyorin-u.ac.jp.
Background:
Plasmodium lacks an mRNA export receptor ortholog, such as yeast Mex67. Yeast Mex67 contains a nuclear transport factor 2 (NTF2)-like domain, suggesting that NTF2-like domain-containing proteins might be associated with mRNA export in Plasmodium. In this study, the relationship between mRNA export and an NTF2-like domain-containing protein, PBANKA_1019700, was investigated using the ANKA strain of rodent malaria parasite Plasmodium berghei.
Methods:
The deletion mutant Δ1019700 was generated by introducing gene-targeting vectors into the P. berghei ANKA genome, and parasite growth and virulence were examined. To investigate whether PBANKA_1019700 is involved in mRNA export, live-cell fluorescence imaging and immunoprecipitation coupled to mass spectrometry (IP-MS) were performed using transgenic parasites expressing fusion proteins (1019700::mCherry).
Results:
Deletion of PBANKA_1019700 affected the sexual phase but not the asexual phase of malaria parasites. Live-cell fluorescence imaging showed that PBANKA_1019700 localizes to the cytoplasm. Moreover, IP-MS analysis of 1019700::mCherry indicated that PBANKA_1019700 interacts with ubiquitin-related proteins but not nuclear proteins.
Conclusions:
PBANKA_1019700 is a noncanonical NTF2-like superfamily protein.
Insights
Plasmodium parasites lack a known mRNA export receptor. Researchers studied PBANKA_1019700, an NTF2-like protein, finding it localizes to the cytoplasm and interacts with ubiquitin proteins, impacting the parasite's sexual phase.
Area of Science:
- Molecular biology
- Parasitology
- Cell biology
Background:
- Plasmodium parasites lack a direct ortholog to yeast mRNA export receptor Mex67.
- The presence of a nuclear transport factor 2 (NTF2)-like domain in Mex67 suggests related proteins may mediate mRNA export in Plasmodium.
- PBANKA_1019700 is an NTF2-like domain-containing protein in Plasmodium berghei.
Purpose of the Study:
- To investigate the role of PBANKA_1019700 in mRNA export in Plasmodium berghei.
- To determine the localization and interaction partners of PBANKA_1019700.
- To assess the impact of PBANKA_1019700 deletion on parasite growth and virulence.
Main Methods:
- Generation of a deletion mutant (Δ1019700) in Plasmodium berghei ANKA.
- Live-cell fluorescence imaging of transgenic parasites expressing PBANKA_1019700::mCherry fusion protein.
- Immunoprecipitation coupled to mass spectrometry (IP-MS) to identify protein interactions.
Main Results:
- Deletion of PBANKA_1019700 specifically affected the sexual phase, not the asexual phase, of malaria parasite development.
- Live-cell imaging revealed that PBANKA_1019700 predominantly localizes to the cytoplasm.
- IP-MS analysis demonstrated that PBANKA_1019700 interacts with ubiquitin-related proteins, not nuclear proteins.
Conclusions:
- PBANKA_1019700 functions as a noncanonical member of the NTF2-like superfamily.
- The protein's cytoplasmic localization and interaction with ubiquitin proteins suggest a role beyond canonical mRNA export.
- Further research is needed to elucidate the precise function of PBANKA_1019700 in Plasmodium sexual development.
Related Concept Videos
ABC Transporters: Exporter
Nuclear Protein Sorting
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
Regulation of Nuclear Protein Sorting
Protein Transport to the Inner Chloroplast Membrane
Protein Transport to the Outer Chloroplast Membrane
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
Directionality of Nuclear Transport

