↓ Skip to main content

Differential Phosphorylation of Ribosomal Proteins in Arabidopsis thaliana Plants during Day and Night

Overview of attention for article published in PLOS ONE, December 2011
Altmetric Badge

About this Attention Score

  • Average Attention Score compared to outputs of the same age
  • Average Attention Score compared to outputs of the same age and source

Mentioned by

twitter
3 X users

Citations

dimensions_citation
52 Dimensions

Readers on

mendeley
72 Mendeley
You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output. Click here to find out more.
Title
Differential Phosphorylation of Ribosomal Proteins in Arabidopsis thaliana Plants during Day and Night
Published in
PLOS ONE, December 2011
DOI 10.1371/journal.pone.0029307
Pubmed ID
Authors

Maria V. Turkina, Hanna Klang Årstrand, Alexander V. Vener

Abstract

Protein synthesis in plants is characterized by increase in the translation rates for numerous proteins and central metabolic enzymes during the day phase of the photoperiod. The detailed molecular mechanisms of this diurnal regulation are unknown, while eukaryotic protein translation is mainly controlled at the level of ribosomal initiation complexes, which also involves multiple events of protein phosphorylation. We characterized the extent of protein phosphorylation in cytosolic ribosomes isolated from leaves of the model plant Arabidopsis thaliana harvested during day or night. Proteomic analyses of preparations corresponding to both phases of the photoperiod detected phosphorylation at eight serine residues in the C-termini of six ribosomal proteins: S2-3, S6-1, S6-2, P0-2, P1 and L29-1. This included previously unknown phosphorylation of the 40S ribosomal protein S6 at Ser-231. Relative quantification of the phosphorylated peptides using stable isotope labeling and mass spectrometry revealed a 2.2 times increase in the day/night phosphorylation ratio at this site. Phosphorylation of the S6-1 and S6-2 variants of the same protein at Ser-240 increased by the factors of 4.2 and 1.8, respectively. The 1.6 increase in phosphorylation during the day was also found at Ser-58 of the 60S ribosomal protein L29-1. It is suggested that differential phosphorylation of the ribosomal proteins S6-1, S6-2 and L29-1 may contribute to modulation of the diurnal protein synthesis in plants.

X Demographics

X Demographics

The data shown below were collected from the profiles of 3 X users who shared this research output. Click here to find out more about how the information was compiled.
Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 72 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 1 1%
Unknown 71 99%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 21 29%
Researcher 18 25%
Student > Master 8 11%
Student > Bachelor 6 8%
Professor > Associate Professor 4 6%
Other 6 8%
Unknown 9 13%
Readers by discipline Count As %
Agricultural and Biological Sciences 33 46%
Biochemistry, Genetics and Molecular Biology 23 32%
Computer Science 2 3%
Engineering 2 3%
Medicine and Dentistry 1 1%
Other 1 1%
Unknown 10 14%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 2. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 19 December 2011.
All research outputs
#14,722,660
of 22,659,164 outputs
Outputs from PLOS ONE
#122,851
of 193,435 outputs
Outputs of similar age
#158,464
of 241,496 outputs
Outputs of similar age from PLOS ONE
#1,673
of 2,973 outputs
Altmetric has tracked 22,659,164 research outputs across all sources so far. This one is in the 32nd percentile – i.e., 32% of other outputs scored the same or lower than it.
So far Altmetric has tracked 193,435 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 15.0. This one is in the 33rd percentile – i.e., 33% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 241,496 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 32nd percentile – i.e., 32% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 2,973 others from the same source and published within six weeks on either side of this one. This one is in the 41st percentile – i.e., 41% of its contemporaries scored the same or lower than it.