Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Functional Analysis of the Hsp93/ClpC Chaperone at the Chloroplast Envelope.

Plant physiology - 1 Jan 2016

Flores-Pérez Úrsula, Bédard Jocelyn, Tanabe Noriaki, Lymperopoulos Panagiotis, Clarke Adrian K, Jarvis Paul

Abstract excerpt

The Hsp100-type chaperone Hsp93/ClpC has crucial roles in chloroplast biogenesis. In addition to its role in proteolysis in the stroma, biochemical and genetic evidence led to the hypothesis that this chaperone collaborates with the inner envelope TIC complex to power preprotein import. Recently, it was suggested that Hsp93, working together with the Clp proteolytic core, can confer a protein quality control...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Arabidopsis Proteins
Share to Chloroplast Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chloroplasts

Share to Endopeptidase Clp

Share to Heat-Shock Proteins

Share to Molecular Chaperones

Share to Plants, Genetically Modified

Share to Protein Transport

Source

Open in PubMed Open full text

Identifiers

PMID: 26586836
DOI: 10.1104/pp.15.01538
PMCID: PMC4704595

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional Analysis of the Hsp93/ClpC Chaperone at the Chloroplast Envelope.PMID 26586836Read ↗

The amino-terminal domain of chloroplast Hsp93 is important for its membrane association and functions in vivo.Semantic proximity Read ↗

A stromal Hsp100 protein is required for normal chloroplast development and function in Arabidopsis.Semantic proximity Read ↗

Further in vivo studies on the role of the molecular chaperone, Hsp93, in plastid protein import.Semantic proximity Read ↗

Stromal Hsp70 is important for protein translocation into pea and Arabidopsis chloroplasts.Semantic proximity Read ↗

In vivo studies on the roles of Tic110, Tic40 and Hsp93 during chloroplast protein import.Semantic proximity Read ↗

The HSP90 chaperone complex, an emerging force in plant development and phenotypic plasticity.Semantic proximity Read ↗

Inactivation of the clpC1 gene encoding a chloroplast Hsp100 molecular chaperone causes growth retardation, leaf chlorosis, lower photosynthetic activity, and a specific reduction in photosystem content.Semantic proximity Read ↗

ATP requirement for chloroplast protein import is set by the Km for ATP hydrolysis of stromal Hsp70 in Physcomitrella patens.Semantic proximity Read ↗

Modified Clp protease complex in the ClpP3 null mutant and consequences for chloroplast development and function in Arabidopsis.Semantic proximity Read ↗

Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70.Semantic proximity Read ↗

The chloroplast clpP gene, encoding a proteolytic subunit of ATP-dependent protease, is indispensable for chloroplast development in tobacco.Semantic proximity Read ↗

The Hsp90 molecular chaperone complex regulates maltose induction and stability of the Saccharomyces MAL gene transcription activator Mal63p.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.