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Article

Canonical signal recognition particle components can be bypassed for posttranslational protein targeting in chloroplasts.

The Plant cell - 1 May 2007

Tzvetkova-Chevolleau Tzvetelina, Hutin Claire, Noël Laurent D, Goforth Robyn, Carde Jean-Pierre, Caffarri Stephano, Sinning Irmgard, Groves Matthew, Teulon Jean-Marie, Hoffman Neil E, Henry Ralph, Havaux Michel, Nussaume Laurent

Abstract excerpt

The chloroplast signal recognition particle (cpSRP) and its receptor (cpFtsY) target proteins both cotranslationally and posttranslationally to the thylakoids. This dual function enables cpSRP to utilize its posttranslational activities for targeting a family of nucleus-encoded light-harvesting chlorophyll binding proteins (LHCPs), the most abundant membrane proteins in plants. Previous in vitro experiments...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 17513500
DOI: 10.1105/tpc.106.048959
PMCID: PMC1913721

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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Canonical signal recognition particle components can be bypassed for posttranslational protein targeting in chloroplasts.PMID 17513500Read ↗

Non-identical contributions of two membrane-bound cpSRP components, cpFtsY and Alb3, to thylakoid biogenesis.Semantic proximity Read ↗

Double mutation cpSRP43--/cpSRP54-- is necessary to abolish the cpSRP pathway required for thylakoid targeting of the light-harvesting chlorophyll proteins.Semantic proximity Read ↗

Genetic and Physical Interaction Studies Reveal Functional Similarities between ALBINO3 and ALBINO4 in Arabidopsis.Semantic proximity Read ↗

Suppressors of the Chloroplast Protein Import Mutant tic40 Reveal a Genetic Link between Protein Import and Thylakoid Biogenesis.Semantic proximity Read ↗

Expression of a dominant negative form of cpSRP54 inhibits chloroplast biogenesis in Arabidopsis.Semantic proximity Read ↗

Arabidopsis mutants lacking the 43- and 54-kilodalton subunits of the chloroplast signal recognition particle have distinct phenotypes.Semantic proximity Read ↗

A toc159 import receptor mutant, defective in hydrolysis of GTP, supports preprotein import into chloroplasts.Semantic proximity Read ↗

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

Domain Organization in the 54-kDa Subunit of the Chloroplast Signal Recognition Particle.Semantic proximity Read ↗

Functional divergence of the plastid and cytosolic forms of the 54-kDa subunit of signal recognition particle.Semantic proximity Read ↗

Functional specialization amongst the Arabidopsis Toc159 family of chloroplast protein import receptors.Semantic proximity Read ↗

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