Evidence map›Paper›PMID 15908606›Full record

ArticlePlant physiology2005

Tripeptidyl peptidase II. An oligomeric protease complex from Arabidopsis.

Adam J Book, Peizhen Yang, Mark Scalf, Lloyd M Smith, Richard D Vierstra

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.5field-weighted citation impact, top 19% of its field
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

24 citing papers in PubMed, 54 citations in OpenAlex.

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  14. Mining the Active Proteome of Arabidopsis thaliana.Frontiers in plant science · 2011
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  18. Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3.Proceedings of the National Academy of Sciences of the United States of America · 2009
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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

5 authors at 1 institution in 1 country.

Adam J BookDepartment of Genetics , University of Wisconsin, Madison, Wisconsin 53706, USA.
Peizhen Yang
Mark Scalf
Lloyd M Smith
Richard D Vierstra
University of Wisconsin–Madison · US

Funding

NHLBI NIH HHS N01-HV-28182
6 · The paper itself

Abstract

The breakdown of most nuclear and cytoplasmic proteins involves their partial cleavage by the 26S proteasome followed by further disassembly to free amino acids by the combined action of endo- and exopeptidases. In animals, one important intermediate exopeptidase is tripeptidyl peptidase (TPP)II, which digests peptide products of the 26S proteasome and other endopeptidases into tripeptides. Here, we describe the purification and characterization of TPPII from Arabidopsis (Arabidopsis thaliana). Like its animal counterparts, Arabidopsis TPPII exists as a soluble, approximately 5- to 9-MD complex. Two related species of 153 and 142 kD are present in the purified preparations that are derived from a single TPP2 gene. Sequencing by Edman degradation of the intact polypeptides and mass spectrometry of proteolytic fragments demonstrated that the 142-kD form mainly differs from the 153-kD form by a truncation at the C-terminal end. This serine protease is a member of the subtilisin superfamily and is sensitive to the inhibitors alanine-alanine-phenylalanine-chloromethylketone and butabindide, which are diagnostic for the TPPII subfamily. The Arabidopsis TPP2 gene is widely expressed in many tissue types with related genes evident in other plant genomes. Whereas the 26S proteasome is essential, TPPII appears not as important for plant physiology. An Arabidopsis T-DNA mutant defective in TPP2 expression displays no phenotypic abnormalities and is not hypersensitive to either amino acid analogs or the 26S proteasome inhibitor MG132. As a consequence, plants likely contain other intermediate exopeptidases that assist in amino acid recycling.

Indexed as

Amino Acid SequenceAminopeptidasesArabidopsisArabidopsis ProteinsChromosome MappingChromosomes, PlantDipeptidyl-Peptidases and Tripeptidyl-PeptidasesMolecular Sequence DataMultienzyme ComplexesMutationSequence Homology, Amino AcidSerine EndopeptidasesAminopeptidasesArabidopsis ProteinsDipeptidyl-Peptidases and Tripeptidyl-PeptidasesMultienzyme ComplexesSerine Endopeptidasestripeptidyl-peptidase 2

Identifiers

PMID15908606
PMCPMC1150419
OpenAlexW2013275817

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.