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

Stromal Hsp70 is important for protein translocation into pea and Arabidopsis chloroplasts.

The Plant cell - 1 May 2010

Su Pai-Hsiang, Li Hsou-min

Abstract excerpt

Hsp70 family proteins function as motors driving protein translocation into mitochondria and the endoplasmic reticulum. Whether Hsp70 is involved in protein import into chloroplasts has not been resolved. We show here Arabidopsis thaliana knockout mutants of either of the two stromal cpHsc70s, cpHsc70-1 and cpHsc70-2, are defective in protein import into chloroplasts during early developmental stages. Protein...

Read the complete abstract on PubMed

Topics

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

Share to Anthocyanins
Share to Chloroplasts
Share to Cross-Linking Reagents

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HSP70 Heat-Shock Proteins

Share to Immunoprecipitation

Share to Photosynthesis

Share to Pisum sativum

Share to Protein Precursors

Source

Open in PubMed Open full text

Identifiers

PMID: 20484004
DOI: 10.1105/tpc.109.071415
PMCID: PMC2899880

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

Stromal Hsp70 is important for protein translocation into pea and Arabidopsis chloroplasts.PMID 20484004Read ↗

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

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

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

Functional Analysis of the Hsp93/ClpC Chaperone at the Chloroplast Envelope.Semantic proximity Read ↗

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

Toc33 and Toc64-III cooperate in precursor protein import into the chloroplasts of Arabidopsis thaliana.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 ↗

Arabidopsis tic110 is essential for the assembly and function of the protein import machinery of plastids.Semantic proximity Read ↗

Impaired expression of chloroplast HSP90C chaperone activates plant defense responses leading to a disease symptom-like phenotypeSemantic proximity Read ↗

Pea chloroplast DnaJ-J8 and Toc12 are encoded by the same gene and localized in the stroma.Semantic proximity Read ↗

The cytosolic/nuclear HSC70 and HSP90 molecular chaperones are important for stomatal closure and modulate abscisic acid-dependent physiological responses in Arabidopsis.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 ↗

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