Evidence map›Paper›PMID 11352464›Full record

ArticlePlant molecular biology2001

Plant mitochondria contain proteolytic and regulatory subunits of the ATP-dependent Clp protease.

T Halperin, B Zheng, H Itzhaki, A K Clarke, Z Adam

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Article in Plant molecular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 74 citations in OpenAlex.

  1. Elucidating the Molecular Impact of DA29-Induced ClpP Chemoactivation on Mitochondrial Function.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
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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 2 institutions in 2 countries.

T HalperinDepartment of Agricultural Botany, Faculty of Agriculture, Hebrew University of Jerusalem, Rehovot, Israel.
B Zheng
H Itzhaki
A K Clarke
Z Adam
Hebrew University of Jerusalem · ILUmeå Plant Science Centre · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The proteolytic machinery of plant organelles is largely unknown, although indications so far point to several proteases of bacterial origin. In this study an Arabidopsis thaliana cDNA was isolated that encodes a homologue of bacterial ClpX, a molecular chaperone and regulatory subunit of the ATP-dependent, serine-type Clp protease. Computer analysis of the predicted plant ClpX revealed a putative mitochondrial transit peptide at the N-terminus, as well as overall sequence similarity to other eukaryotic ClpX homologues. Specific polyclonal antibodies were made to the Arabidopsis ClpX protein and used to confirm its localization in plant mitochondria. In addition to ClpX, a ClpP protein located in mitochondria was also identified from the numerous ClpP isomers in Arabidopsis. Localization of this nuclear-encoded protein, termed ClpP2, was determined first by its close sequence similarity to mitochondrial ClpP human, and later experimentally using ClpP2-specific antibodies with isolated plant organellar fractions. In Arabidopsis, transcripts for both clpX and clpP2 genes were detected in various tissues and under different growth conditions, with no significant variation in mRNA level (i.e. 2-fold) for each gene between samples. Using beta-casein as a substrate, plant mitochondria were found to possess an ATP-stimulated, serine-type proteolytic activity that could be strongly inhibited by antibodies specific for ClpX or ClpP2, suggesting an active ClpXP protease. The recent discovery of homologous mitochondrial ClpX and ClpP proteins in mammals suggests that this type of protease may be common to multicellular eukaryotes.

Indexed as

Bacterial ProteinsAdenosine TriphosphatasesAmino Acid SequenceArabidopsisATPases Associated with Diverse Cellular ActivitiesCaseinsDNA, ComplementaryEndopeptidase ClpEscherichia coli ProteinsGene Expression Regulation, EnzymologicGene Expression Regulation, PlantMitochondriaMolecular ChaperonesMolecular Sequence DataPhylogenyProtein SubunitsAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesBacterial ProteinsCaseinsClpP2 protein, bacteriaClpX protein, E coliDNA, ComplementaryEndopeptidase ClpEscherichia coli ProteinsMolecular ChaperonesProtein SubunitsRNA, MessengerSerine Endopeptidases

Identifiers

PMID11352464
OpenAlexW1608825978

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.