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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

Co-fractionation of NSN1 with ribosome subunits. (A) GFP fusion proteins of NSN1, NSN1-N, and EBP2 were expressed in N. benthamiana leaves by agroinfiltration. After sedimentation of ribosomes through a sucrose density gradient, the fractions were analysed by immunoblotting with anti-GFP and anti-ribosomal protein L10a (RPL10a) antibodies. Lanes 1–27 indicate the gradient fractions from the top (5%) to the bottom (35%). Positions of 40S small subunits, 60S large subunits, and 80S monosomes are indicated. RPL10a is present in 60S large subunits and 80S monosomes. (B) NSN1:GFP was expressed in N. benthamiana leaves by agroinfiltration. Ribosomal fractions were briefly treated with RNase A before sedimentation through a sucrose density gradient.
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Figure 5: Co-fractionation of NSN1 with ribosome subunits. (A) GFP fusion proteins of NSN1, NSN1-N, and EBP2 were expressed in N. benthamiana leaves by agroinfiltration. After sedimentation of ribosomes through a sucrose density gradient, the fractions were analysed by immunoblotting with anti-GFP and anti-ribosomal protein L10a (RPL10a) antibodies. Lanes 1–27 indicate the gradient fractions from the top (5%) to the bottom (35%). Positions of 40S small subunits, 60S large subunits, and 80S monosomes are indicated. RPL10a is present in 60S large subunits and 80S monosomes. (B) NSN1:GFP was expressed in N. benthamiana leaves by agroinfiltration. Ribosomal fractions were briefly treated with RNase A before sedimentation through a sucrose density gradient.

Mentions: To investigate the association of NSN1 and EBP2 with ribosomes, NSN1, its N-terminal domain (NSN1-N), and EBP2 were expressed as GFP fusion proteins in N. benthamiana leaves by agroinfiltration. Then, leaf cells expressing these proteins were fractionated on a sucrose density gradient. After ultracentrifugation, fractions were collected, and immunoblot analysis was performed with anti-GFP antibodies (Fig. 5A). As a control for fractionation, another immunoblot analysis was performed with antibodies against the 60S ribosomal protein L10a (RPL10a). GFP:NSN1, GFP:NSN1-N, and GFP:EBP2 were enriched in fractions that contained 60S large subunits and 80S monosomes, suggesting that NSN1 and EBP2 may associate with ribosomes (Fig. 5A). These results also suggest that the NSN1 N-terminal region is important for NSN1 association with ribosomes.


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)

Co-fractionation of NSN1 with ribosome subunits. (A) GFP fusion proteins of NSN1, NSN1-N, and EBP2 were expressed in N. benthamiana leaves by agroinfiltration. After sedimentation of ribosomes through a sucrose density gradient, the fractions were analysed by immunoblotting with anti-GFP and anti-ribosomal protein L10a (RPL10a) antibodies. Lanes 1–27 indicate the gradient fractions from the top (5%) to the bottom (35%). Positions of 40S small subunits, 60S large subunits, and 80S monosomes are indicated. RPL10a is present in 60S large subunits and 80S monosomes. (B) NSN1:GFP was expressed in N. benthamiana leaves by agroinfiltration. Ribosomal fractions were briefly treated with RNase A before sedimentation through a sucrose density gradient.
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Figure 5: Co-fractionation of NSN1 with ribosome subunits. (A) GFP fusion proteins of NSN1, NSN1-N, and EBP2 were expressed in N. benthamiana leaves by agroinfiltration. After sedimentation of ribosomes through a sucrose density gradient, the fractions were analysed by immunoblotting with anti-GFP and anti-ribosomal protein L10a (RPL10a) antibodies. Lanes 1–27 indicate the gradient fractions from the top (5%) to the bottom (35%). Positions of 40S small subunits, 60S large subunits, and 80S monosomes are indicated. RPL10a is present in 60S large subunits and 80S monosomes. (B) NSN1:GFP was expressed in N. benthamiana leaves by agroinfiltration. Ribosomal fractions were briefly treated with RNase A before sedimentation through a sucrose density gradient.
Mentions: To investigate the association of NSN1 and EBP2 with ribosomes, NSN1, its N-terminal domain (NSN1-N), and EBP2 were expressed as GFP fusion proteins in N. benthamiana leaves by agroinfiltration. Then, leaf cells expressing these proteins were fractionated on a sucrose density gradient. After ultracentrifugation, fractions were collected, and immunoblot analysis was performed with anti-GFP antibodies (Fig. 5A). As a control for fractionation, another immunoblot analysis was performed with antibodies against the 60S ribosomal protein L10a (RPL10a). GFP:NSN1, GFP:NSN1-N, and GFP:EBP2 were enriched in fractions that contained 60S large subunits and 80S monosomes, suggesting that NSN1 and EBP2 may associate with ribosomes (Fig. 5A). These results also suggest that the NSN1 N-terminal region is important for NSN1 association with ribosomes.

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