Chloroplast SRP54 Was Recruited for Posttranslational Protein Transport via Complex Formation with Chloroplast SRP43 during Land Plant Evolution

Dünschede, Beatrix; Träger, Chantal; Schröder, Christine Vera; Ziehe, Dominik; Walter, Britta; Funke, Silke; Hofmann, Eckhard; Schünemann, Danja

doi:10.1074/jbc.m114.597922

Cited by 32 publications

(44 citation statements)

References 37 publications

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“…This may represent an adaptive mechanism during organelle evolution, from the ribosome-dependent co-translational insertion to the chaperone-dependent post-translational transport. This is similar to the case with the cpSRP pathway, which has evolved to catalyze post-translational membrane insertion of LHCP during chloroplast evolution with acquisition of a novel chaperone cpSRP43 (69,70). Together, these findings emphasize the flexibility of protein transport mechanisms.…”

Section: Discussionsupporting

confidence: 54%

Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1

Endow

Singhal

Fernandez

et al. 2015

Journal of Biological Chemistry

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Background:In bacteria, type I signal peptidase is targeted to the membrane co-translationally. Results: Plastidic type I signal peptidase 1 (Plsp1) could insert into the membrane in an incorrect orientation, which was prevented by a stroma chaperone and the cpSec1 machine. Conclusion: Correct membrane insertion of Plsp1 is ensured by stromal components.Significance: The results demonstrate an adaptive mechanism of protein transport during organelle evolution.

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Section: Discussionsupporting

confidence: 54%

Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1

Endow

Singhal

Fernandez

et al. 2015

Journal of Biological Chemistry

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“…The moss Physcomitrella patens , for example, contains a cpSRP RNA with an elongated apical loop instead of the classical tetraloop, which is typically present in bacterial SRP RNAs [9, 17] (Fig 1B). Interestingly, a recent study demonstrated that the cpSRP system in chlorophytes (e.g., Chlamydomonas reinhardtii ) differs from that of land plants in that cpSRP43 is not complexed to cpSRP54 ([15], Fig 1A). The inability of the cpSRP complex formation is due to alterations within the cpSRP54 C-terminal tail region and the second chromodomain (CD2) of cpSRP43, which form the binding interface in Arabidopsis thaliana .…”

Section: Introductionmentioning

confidence: 99%

“…The inability of the cpSRP complex formation is due to alterations within the cpSRP54 C-terminal tail region and the second chromodomain (CD2) of cpSRP43, which form the binding interface in Arabidopsis thaliana . Here, CD2 forms two aromatic cages that are crucial for recognizing the cpSRP43-binding motif ARR that is located in close proximity to the C-terminus of cpSRP54 [15, 18, 19] (Fig 1C and 1D). The cpSRP54 tail of chlorophytes (e.g., Chlamydomonas reinhardtii ) does not contain the within streptophytes conserved cpSRP43-binding motif A(R/K)R but displays a valine instead of an alanine, which interferes with cpSRP43 binding [15] (Fig 1C).…”

Section: Introductionmentioning

confidence: 99%

“…Here, CD2 forms two aromatic cages that are crucial for recognizing the cpSRP43-binding motif ARR that is located in close proximity to the C-terminus of cpSRP54 [15, 18, 19] (Fig 1C and 1D). The cpSRP54 tail of chlorophytes (e.g., Chlamydomonas reinhardtii ) does not contain the within streptophytes conserved cpSRP43-binding motif A(R/K)R but displays a valine instead of an alanine, which interferes with cpSRP43 binding [15] (Fig 1C). The cpSRP43 proteins of chlorophytes differ from cpSRP43 of land plants by displaying a proline in the first β-strand of CD2, which is detrimental to cpSRP54-binding ([15], Fig 1D).…”

Section: Introductionmentioning

confidence: 99%

“…The cpSRP54 tail of chlorophytes (e.g., Chlamydomonas reinhardtii ) does not contain the within streptophytes conserved cpSRP43-binding motif A(R/K)R but displays a valine instead of an alanine, which interferes with cpSRP43 binding [15] (Fig 1C). The cpSRP43 proteins of chlorophytes differ from cpSRP43 of land plants by displaying a proline in the first β-strand of CD2, which is detrimental to cpSRP54-binding ([15], Fig 1D). The inability of cpSRP54 to bind cpSRP43 in chlorophytes has a significant impact on its function because the involvement of cpSRP54 in transit complex formation is dependent on the interaction with cpSRP43 [15].…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2016

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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.

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PALE‐GREEN LEAF 1, a rice cpSRP54 protein, is essential for the assembly of the PSI‐LHCI supercomplex

Gao

Xia

et al. 2022

Plant Direct

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Although photosynthetic multiprotein complexes have received major attention, our knowledge about the assembly of these proteins into functional complexes in plants is still limited. In the present study, we have identified a chlorophyll‐deficient mutant, pale ‐ green leaf 1 ( pgl1 ), in rice that displays abnormally developed chloroplasts. Map‐based cloning of this gene revealed that OsPGL1 encodes a chloroplast targeted protein homologous to the 54‐kDa subunit of the signal recognition particle (cpSRP54). Immunoblot analysis revealed that the accumulation of the PSI core proteins PsaA and PsaB, subunits from the ATP synthase, cytochrome, and light‐harvesting complex (LHC) is dramatically reduced in pgl1 . Blue native gel analysis of thylakoid membrane proteins showed the existence of an extra band in the pgl1 mutant, which located between the dimeric PSII/PSI‐LHCI and the monomeric PSII. Immunodetection after 2D separation indicated that the extra band consists of the proteins from the PSI core complex. Measurements of chlorophyll fluorescence at 77 K further confirmed that PSI, rather than PSII, was primarily impaired in the pgl1 mutant. These results suggest that OsPGL1 might act as a molecular chaperone that is required for the efficient assembly and specific integration of the peripheral LHCI proteins into the PSI core complex in rice.

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Chloroplast SRP54 Was Recruited for Posttranslational Protein Transport via Complex Formation with Chloroplast SRP43 during Land Plant Evolution

Cited by 32 publications

References 37 publications

Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1

Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1

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

PALE‐GREEN LEAF 1, a rice cpSRP54 protein, is essential for the assembly of the PSI‐LHCI supercomplex

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