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The nucleolar GTPase nucleostemin-like 1 plays a role in plant growth and senescence by modulating ribosome biogenesis.

Jeon Y, Park YJ, Cho HK, Jung HJ, Ahn TK, Kang H, Pai HS - J. Exp. Bot. (2015)

Bottom Line: Depletion of NSN1 delayed 25S rRNA maturation and biogenesis of the 60S ribosome subunit, and repressed global translation.NSN1-deficient plants exhibited premature leaf senescence, excessive accumulation of reactive oxygen species, and senescence-related gene expression.Taken together, these results suggest that NSN1 plays a crucial role in plant growth and senescence by modulating ribosome biogenesis.

View Article: PubMed Central - PubMed

Affiliation: Department of Systems Biology, Yonsei University, Seoul 120-749, Korea.

No MeSH data available.


Related in: MedlinePlus

Subcellular localization of Arabidopsis NSN1 and its deletion mutants. (A) Schematic of NSN1 and NSN1 deletion mutants. B, basic domain (amino acids 1–93); CC, coiled-coil domain (amino acids58–80); DAR, the DAR motif (amino acids 145–147), G4–G3, GTP-binding motifs (amino acids 175–307); and A, acidic domain (amino acids 471–570). Amino acid (aa) residues at deletion points are marked. Asterisks indicate nuclear localization signals. (B) Subcellular localization of NSN1 and NSN1 deletion mutants using GFP fusion. GFP fusion proteins were expressed in N. benthamiana leaves via agroinfiltration, and protoplasts prepared from the infiltrated leaves were observed by confocal laser scanning microscopy for GFP fluorescence and chlorophyll autofluorescence. Protoplasts expressing GFP:NSN1 were stained with 4′,6-diamidino-2-phenylindole (DAPI) to visualize the nucleus. (C) Effects of mycophenolic acid (MPA) on the localization of NSN1 and NSN1 deletion mutants. Nictiana benthamiana leaves were agroinfiltrated with GFP fusion constructs and then treated with MPA (20 μM) for 12h. Nuclei were visualized by DAPI staining. (This figure is available in colour at JXB online.)
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Figure 2: Subcellular localization of Arabidopsis NSN1 and its deletion mutants. (A) Schematic of NSN1 and NSN1 deletion mutants. B, basic domain (amino acids 1–93); CC, coiled-coil domain (amino acids58–80); DAR, the DAR motif (amino acids 145–147), G4–G3, GTP-binding motifs (amino acids 175–307); and A, acidic domain (amino acids 471–570). Amino acid (aa) residues at deletion points are marked. Asterisks indicate nuclear localization signals. (B) Subcellular localization of NSN1 and NSN1 deletion mutants using GFP fusion. GFP fusion proteins were expressed in N. benthamiana leaves via agroinfiltration, and protoplasts prepared from the infiltrated leaves were observed by confocal laser scanning microscopy for GFP fluorescence and chlorophyll autofluorescence. Protoplasts expressing GFP:NSN1 were stained with 4′,6-diamidino-2-phenylindole (DAPI) to visualize the nucleus. (C) Effects of mycophenolic acid (MPA) on the localization of NSN1 and NSN1 deletion mutants. Nictiana benthamiana leaves were agroinfiltrated with GFP fusion constructs and then treated with MPA (20 μM) for 12h. Nuclei were visualized by DAPI staining. (This figure is available in colour at JXB online.)

Mentions: NSN1 contains a predicted basic domain (B), a coiled-coil domain (CC), the DAR motif, the GTP-binding motifs (G4, G1, and G3), and an acidic domain (A) (Fig. 2A; Supplementary Fig. S1 at JXB online). Multiple nuclear localization signals are located in both the N- and C-terminal regions, which are marked with asterisks. To determine the subcellular localization of NSN1, GFP fusion proteins of Arabidopsis NSN1 and NSN1-deletion mutants were expressed in N. benthamiana leaves via agroinfiltration. GFP was fused to the N-termini of NSN1 and its derivatives. However, the N-terminal deletion form (∆N) and the C-terminal region (NSN1-C) were more stable when fused to GFP via their C-termini. Confocal laser scanning microscopy of leaf protoplasts revealed that GFP:NSN1 was predominantly localized to the nucleolus (Fig. 2B; Supplementary Fig. S4). Deletion of the GTP-binding motifs G4–G3 (∆GD) or the C-terminal region (∆C) did not affect NSN1 nucleolar localization (Fig. 2B). However, deletion of the N-terminal 94 amino acids (∆N) resulted in NSN1 distribution in the nucleus and the cytosol (Fig. 2B; Supplementary Fig. S4). The deletion mutant lacking the N-terminal 174 amino acids was not stably expressed in N. bethamiana leaves, regardless of the position of GFP tagging. The N-terminus (NSN1-N; amino acid residues 1–174) was sufficient to target the GFP fusion protein to the nucleolus. The GFP fusion protein containing the NSN1 C-terminal region (NSN1-C; amino acids 318–582) localized to both the nucleus and the cytosol (Fig. 2B; Supplementary Fig. S5). This result suggests that the NSN1 N-terminal region is crucial for NSN1 nucleolar localization.


The nucleolar GTPase nucleostemin-like 1 plays a role in plant growth and senescence by modulating ribosome biogenesis.

Jeon Y, Park YJ, Cho HK, Jung HJ, Ahn TK, Kang H, Pai HS - J. Exp. Bot. (2015)

Subcellular localization of Arabidopsis NSN1 and its deletion mutants. (A) Schematic of NSN1 and NSN1 deletion mutants. B, basic domain (amino acids 1–93); CC, coiled-coil domain (amino acids58–80); DAR, the DAR motif (amino acids 145–147), G4–G3, GTP-binding motifs (amino acids 175–307); and A, acidic domain (amino acids 471–570). Amino acid (aa) residues at deletion points are marked. Asterisks indicate nuclear localization signals. (B) Subcellular localization of NSN1 and NSN1 deletion mutants using GFP fusion. GFP fusion proteins were expressed in N. benthamiana leaves via agroinfiltration, and protoplasts prepared from the infiltrated leaves were observed by confocal laser scanning microscopy for GFP fluorescence and chlorophyll autofluorescence. Protoplasts expressing GFP:NSN1 were stained with 4′,6-diamidino-2-phenylindole (DAPI) to visualize the nucleus. (C) Effects of mycophenolic acid (MPA) on the localization of NSN1 and NSN1 deletion mutants. Nictiana benthamiana leaves were agroinfiltrated with GFP fusion constructs and then treated with MPA (20 μM) for 12h. Nuclei were visualized by DAPI staining. (This figure is available in colour at JXB online.)
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Figure 2: Subcellular localization of Arabidopsis NSN1 and its deletion mutants. (A) Schematic of NSN1 and NSN1 deletion mutants. B, basic domain (amino acids 1–93); CC, coiled-coil domain (amino acids58–80); DAR, the DAR motif (amino acids 145–147), G4–G3, GTP-binding motifs (amino acids 175–307); and A, acidic domain (amino acids 471–570). Amino acid (aa) residues at deletion points are marked. Asterisks indicate nuclear localization signals. (B) Subcellular localization of NSN1 and NSN1 deletion mutants using GFP fusion. GFP fusion proteins were expressed in N. benthamiana leaves via agroinfiltration, and protoplasts prepared from the infiltrated leaves were observed by confocal laser scanning microscopy for GFP fluorescence and chlorophyll autofluorescence. Protoplasts expressing GFP:NSN1 were stained with 4′,6-diamidino-2-phenylindole (DAPI) to visualize the nucleus. (C) Effects of mycophenolic acid (MPA) on the localization of NSN1 and NSN1 deletion mutants. Nictiana benthamiana leaves were agroinfiltrated with GFP fusion constructs and then treated with MPA (20 μM) for 12h. Nuclei were visualized by DAPI staining. (This figure is available in colour at JXB online.)
Mentions: NSN1 contains a predicted basic domain (B), a coiled-coil domain (CC), the DAR motif, the GTP-binding motifs (G4, G1, and G3), and an acidic domain (A) (Fig. 2A; Supplementary Fig. S1 at JXB online). Multiple nuclear localization signals are located in both the N- and C-terminal regions, which are marked with asterisks. To determine the subcellular localization of NSN1, GFP fusion proteins of Arabidopsis NSN1 and NSN1-deletion mutants were expressed in N. benthamiana leaves via agroinfiltration. GFP was fused to the N-termini of NSN1 and its derivatives. However, the N-terminal deletion form (∆N) and the C-terminal region (NSN1-C) were more stable when fused to GFP via their C-termini. Confocal laser scanning microscopy of leaf protoplasts revealed that GFP:NSN1 was predominantly localized to the nucleolus (Fig. 2B; Supplementary Fig. S4). Deletion of the GTP-binding motifs G4–G3 (∆GD) or the C-terminal region (∆C) did not affect NSN1 nucleolar localization (Fig. 2B). However, deletion of the N-terminal 94 amino acids (∆N) resulted in NSN1 distribution in the nucleus and the cytosol (Fig. 2B; Supplementary Fig. S4). The deletion mutant lacking the N-terminal 174 amino acids was not stably expressed in N. bethamiana leaves, regardless of the position of GFP tagging. The N-terminus (NSN1-N; amino acid residues 1–174) was sufficient to target the GFP fusion protein to the nucleolus. The GFP fusion protein containing the NSN1 C-terminal region (NSN1-C; amino acids 318–582) localized to both the nucleus and the cytosol (Fig. 2B; Supplementary Fig. S5). This result suggests that the NSN1 N-terminal region is crucial for NSN1 nucleolar localization.

Bottom Line: Depletion of NSN1 delayed 25S rRNA maturation and biogenesis of the 60S ribosome subunit, and repressed global translation.NSN1-deficient plants exhibited premature leaf senescence, excessive accumulation of reactive oxygen species, and senescence-related gene expression.Taken together, these results suggest that NSN1 plays a crucial role in plant growth and senescence by modulating ribosome biogenesis.

View Article: PubMed Central - PubMed

Affiliation: Department of Systems Biology, Yonsei University, Seoul 120-749, Korea.

No MeSH data available.


Related in: MedlinePlus