Evidence map›Paper›PMID 20516081›Full record

ArticleThe Journal of biological chemistry2010

Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse array of plant proteolytic complexes.

Adam J Book, Nicholas P Gladman, Sang-Sook Lee, Mark Scalf, Lloyd M Smith, Richard D Vierstra

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

81 citing papers in PubMed.

  1. Article
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  19. Review
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21 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Adam J BookDepartment of Genetics, University of Wisconsin, Madison, Wisconsin 53706, USA.
Nicholas P Gladman
Sang-Sook Lee
Mark Scalf
Lloyd M Smith
Richard D Vierstra

Funding

Wisconsin Center of Excellence in Genomics ScienceP50HG004952 · NHGRI · TEXAS BIOMEDICAL RESEARCH INSTITUTE · PI OLIVIER, MICHAEL · 2009 to 2013
$13.0M
Diversity-Oriented Synthesis of Novel Heterocyclic & Natural Product-Like LibraryP41GM081269 · NIGMS · FLUOROUS TECHNOLOGIES, INC. · PI YU, MARVIN S · 2007 to 2009
$1.6M
Compositional Analysis of the Arabidopsis 26S ProteasomeF31NS054563 · NINDS · UNIVERSITY OF WISCONSIN-MADISON · PI BOOK, ADAM J · 2006 to 2009
$136k
NHGRI NIH HHS 1P50HG004952NHGRI NIH HHS P50 HG004952NIGMS NIH HHS P01GM081269NIGMS NIH HHS P41 GM081269NINDS NIH HHS F31 NS054563
6 · The paper itself

Abstract

Selective proteolysis in plants is largely mediated by the ubiquitin (Ub)/proteasome system in which substrates, marked by the covalent attachment of Ub, are degraded by the 26 S proteasome. The 26 S proteasome is composed of two subparticles, the 20 S core protease (CP) that compartmentalizes the protease active sites and the 19 S regulatory particle that recognizes and translocates appropriate substrates into the CP lumen for breakdown. Here, we describe an affinity method to rapidly purify epitope-tagged 26 S proteasomes intact from Arabidopsis thaliana. In-depth mass spectrometric analyses of preparations generated from young seedlings confirmed that the 2.5-MDa CP-regulatory particle complex is actually a heterogeneous set of particles assembled with paralogous pairs for most subunits. A number of these subunits are modified post-translationally by proteolytic processing, acetylation, and/or ubiquitylation. Several proteasome-associated proteins were also identified that likely assist in complex assembly and regulation. In addition, we detected a particle consisting of the CP capped by the single subunit PA200 activator that may be involved in Ub-independent protein breakdown. Taken together, it appears that a diverse and highly dynamic population of proteasomes is assembled in plants, which may expand the target specificity and functions of intracellular proteolysis.

Indexed as

ArabidopsisArabidopsis ProteinsChromatography, High Pressure LiquidElectrophoresis, Polyacrylamide GelMass SpectrometryProteasome Endopeptidase ComplexSpectrometry, Mass, Electrospray IonizationTandem Mass SpectrometryArabidopsis ProteinsProteasome Endopeptidase Complex

Identifiers

PMID20516081
PMCPMC2919120

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.