Paper · 2016 · PLoS ONE

The Chloroplast SRP Systems of Chaetosphaeridium globosum and Physcomitrella patens as Intermediates in the Evolution of SRP-Dependent Protein Transport in Higher Plants

Dominik Ziehe; Beatrix Dünschede; Mira Zenker; et al.

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claims
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verbatim quotes
3
citations
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research areas
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Open access · cc-by

Abstract

The bacterial signal recognition particle (SRP) mediates the cotranslational targeting of membrane proteins and is a high affinity complex consisting of a SRP54 protein subunit (Ffh) and an SRP RNA. The chloroplast SRP (cpSRP) pathway has adapted throughout evolution to enable the posttranslational targeting of the light harvesting chlorophyll a/b binding proteins (LHCPs) to the thylakoid membrane. In spermatophytes (seed plants), the cpSRP lacks the SRP RNA and is instead formed by a high affinity interaction of the conserved 54-kD subunit (cpSRP54) with the chloroplast-specific cpSRP43 protein. This heterodimeric cpSRP recognizes LHCP and delivers it to the thylakoid membrane. However, in contrast to spermatophytes, plastid SRP RNAs were identified within all streptophyte lineages and in all chlorophyte branches. Furthermore, it was shown that cpSRP43 does not interact with cpSRP54 in chlorophytes (e.g., Chlamydomonas reinhardtii). In this study, we biochemically characterized the cpSRP system of the charophyte Chaetosphaeridium globosum and the bryophyte Physcomitrella patens. Interaction studies demonstrate low affinity binding of cpSRP54 to cpSRP43 (Kd ~10 μM) in Chaetosphaeridium globosum and Physcomitrella patens as well as relatively low affinity binding of cpSRP54 to cpSRP RNA (Kd ~1 μM) in Physcomitrella patens. CpSRP54/cpSRP43 complex formation in charophytes is supported by the finding that specific alterations in the second chromodomain of cpSRP43, that are conserved within charophytes and absent in land plants, do not interfere with cpSRP54 binding. Furthermore, our data show that the elongated apical loop structure of the Physcomitrella patens cpSRP RNA contributes to the low binding affinity between cpSRP54 and the cpSRP RNA.

Abstract from the paper’s OpenAlex record; open copy licensed cc-by. Read at the source ↗

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Claims 5

Observationobservedoriginal resultmeasured

Claim · model-written summary

cpSRP54 binds cpSRP43 with low affinity in Chaetosphaeridium globosum.

Taxon
Chaetosphaeridium globosumChaetosphaeridium globosume0
Gene
cpSRP54e0
Outcome
low affinity binding of cpSRP54 to cpSRP43e0
Value
Kd ~10 μMe0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Chaetosphaeridium globosum
Chaetosphaeridium globosum · TaxonPetr Knotek · CC BY 4.0 · Wikimedia Commons ↗

Verbatim

e0

“low affinity binding of cpSRP54 to cpSRP43 (Kd ~10 μM) in Chaetosphaeridium globosum”

✓ located verbatim in the source · abstract, characters 1129–1213 · show in text ↑
Observationobservedoriginal resultmeasured

Claim · model-written summary

cpSRP54 binds cpSRP43 with low affinity in Physcomitrella patens.

Taxon
Physcomitrella patensPhyscomitrium patense0
Gene
cpSRP54e0
Outcome
low affinity binding of cpSRP54 to cpSRP43e0
Value
Kd ~10 μMe0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Physcomitrium patens
Physcomitrium patens · TaxonGeorge Greiff · CC BY 4.0 · iNaturalist ↗

Verbatim

e0

“low affinity binding of cpSRP54 to cpSRP43 (Kd ~10 μM) in Chaetosphaeridium globosum and Physcomitrella patens”

✓ located verbatim in the source · abstract, characters 1129–1239 · show in text ↑
Observationobservedoriginal resultmeasured

Claim · model-written summary

cpSRP54 binds cpSRP RNA with relatively low affinity in Physcomitrella patens.

Taxon
Physcomitrella patensPhyscomitrium patense0
Gene
cpSRP54e0
Outcome
relatively low affinity binding of cpSRP54 to cpSRP RNAe0
Value
Kd ~1 μMe0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Physcomitrium patens
Physcomitrium patens · TaxonGeorge Greiff · CC BY 4.0 · iNaturalist ↗

Verbatim

e0

“relatively low affinity binding of cpSRP54 to cpSRP RNA (Kd ~1 μM) in Physcomitrella patens”

✓ located verbatim in the source · abstract, characters 1251–1342 · show in text ↑
Observationobservedoriginal resultmeasured

Claim · model-written summary

Charophyte cpSRP43 second-chromodomain alterations do not interfere with cpSRP54 binding.

Taxon
Chaetosphaeridium globosumChaetosphaeridium globosumt0
Gene
cpSRP43e0
Outcome
do not interfere with cpSRP54 bindinge0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Chaetosphaeridium globosum
Chaetosphaeridium globosum · TaxonPetr Knotek · CC BY 4.0 · Wikimedia Commons ↗

Verbatim

e0

“specific alterations in the second chromodomain of cpSRP43, that are conserved within charophytes and absent in land plants, do not interfere with cpSRP54 binding”

✓ located verbatim in the source · abstract, characters 1426–1588 · show in text ↑
t0

“Chaetosphaeridium globosum”

✓ located verbatim in the source · title, characters 31–57 · show in text ↑
Mechanismauthor interpretationoriginal resultmeasured

Claim · model-written summary

The elongated apical loop of Physcomitrella patens cpSRP RNA contributes to low affinity for cpSRP54.

Taxon
Physcomitrella patensPhyscomitrium patense0
Gene
cpSRP RNAe0
Outcome
low binding affinity between cpSRP54 and the cpSRP RNAe0
Qualifier
elongated apical loop structuree0

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Physcomitrium patens
Physcomitrium patens · TaxonGeorge Greiff · CC BY 4.0 · iNaturalist ↗

Verbatim

e0

“the elongated apical loop structure of the Physcomitrella patens cpSRP RNA contributes to the low binding affinity between cpSRP54 and the cpSRP RNA”

✓ located verbatim in the source · abstract, characters 1622–1770 · show in text ↑