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Research article
Stefanie J. Mueller-Schuessele
University of Bonn
Corresponding Author
ORCiD: https://orcid.org/0000-0003-4061-1175
License:
This work is licensed under a CC BY 4.0 License. Read Full License
Background: Flexibility of plant metabolism is supported by redox regulation of enzymes via posttranslational modification of cysteine residues, especially in plastids. Here, the redox states of cysteine residues are partly coupled to the thioredoxin system and partly to the glutathione pool for reduction. Moreover, several plastid enzymes involved in reactive oxygen species (ROS) scavenging and damage repair draw electrons from glutathione. In addition, cysteine residues can be post-translationally modified by forming a disulfide with glutathione (S-glutathionylation), which protects thiol groups from further oxidation and can influence protein activity. However, the evolution of the plastid glutathione-dependent redox network in land plants and the conservation of cysteine residues undergoing S-glutathionylation is largely unclear.
Results: We analysed the genomes of nine representative model species from streptophyte algae to angiosperms and find that the components of the plastid glutathione-dependent redox network are largely conserved, except for lambda- and the closely related iota-glutathione S-transferases. Screening the literature for target thiols of S-glutathionylation, we find that 151 plastid proteins have been identified as glutathionylation targets, while the exact cysteine residue is only known for 17% (26 proteins), with one or multiple sites per protein, resulting in 37 known S-glutathionylation sites for plastids. However, 38% (14) of the known sites were completely conserved in model species from green algae to flowering plants, with 22% (8) on non-catalytic cysteines. Variable conservation of the remaining sites indicates independent gains and losses of cysteines at the same position during land plant evolution.
Conclusions: We conclude that the glutathione dependent redox network in plastids is highly conserved in streptophytes with some variability in scavenging and damage repair enzymes. Our analysis of cysteine conservation suggests that S-glutathionylation in plastids plays an important and yet under-investigated role in redox regulation and stress response.
Keywords
Protein S-glutathionylation, redox regulation, land plant evolution, plastid, glutathione, glutaredoxin, glutathione reductase, photosynthesis
Figure 1
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Figure 2
Figure 3
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Figure 4
Figure 4
This is a list of supplementary files associated with this preprint. Click to download.
- Additionalfile10alignmentssites.docx
Word-file (DOCX) containing all alignments used to assess conservation of known S-glutathionylation sites on plastid proteins in fasta format
- Additionalfile10alignmentssites.docx
Word-file (DOCX) containing all alignments used to assess conservation of known S-glutathionylation sites on plastid proteins in fasta format
- Additionalfile11alignmentstrees.docx
Word-file (DOCX) containing all alignments used to build phylogenetic trees in FASTA format.
- Additionalfile11alignmentstrees.docx
Word-file (DOCX) containing all alignments used to build phylogenetic trees in FASTA format.
- Additionalfile12PhylogenetictreesML.docx
Word-file (DOCX) containing phylogenetic trees generated with alternative method (Maximum Likelihood)
- Additionalfile12PhylogenetictreesML.docx
Word-file (DOCX) containing phylogenetic trees generated with alternative method (Maximum Likelihood)
- Additionalfile1TableS1201105.xlsx
Table S1 containing protein model information and targeting predictions (XLSX)
- Additionalfile1TableS1201105.xlsx
Table S1 containing protein model information and targeting predictions (XLSX)
- Additionalfile2DHAR201106.pdf
Phylogenetic tree of DHAR (PDF)
- Additionalfile2DHAR201106.pdf
Phylogenetic tree of DHAR (PDF)
- Additionalfile3GSTLI201106.pdf
Phylogenetic tree of GSTI and GSTL (PDF)
- Additionalfile3GSTLI201106.pdf
Phylogenetic tree of GSTI and GSTL (PDF)
- Additionalfile4MSRB201109.pdf
Phylogenetic tree of MSRB (PDF)
- Additionalfile4MSRB201109.pdf
Phylogenetic tree of MSRB (PDF)
- Additionalfile5PRXIIE200804.pdf
Phylogenetic tree of PRXIIE (PDF)
- Additionalfile5PRXIIE200804.pdf
Phylogenetic tree of PRXIIE (PDF)
- Additionalfile6GRXclass1201106.pdf
Phylogenetic tree of PRXIIE (PDF)
- Additionalfile6GRXclass1201106.pdf
Phylogenetic tree of PRXIIE (PDF)
- Additionalfile7GRXS14S16201106.pdf
Phylogenetic tree of GRXS14 and GRXS16 (PDF)
- Additionalfile7GRXS14S16201106.pdf
Phylogenetic tree of GRXS14 and GRXS16 (PDF)
- Additionalfile8GR200804.pdf
Phylogenetic tree of GR (PDF)
- Additionalfile8GR200804.pdf
Phylogenetic tree of GR (PDF)
- Additionalfile9TableS2200908.xlsx
Table S2 (XLSX) Lists of S-glutathionylation sites and organisms
- Additionalfile9TableS2200908.xlsx
Table S2 (XLSX) Lists of S-glutathionylation sites and organisms
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CURRENT STATUS: Published
View the published article at BMC Plant Biology.
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No community comments so far
Editorial decision: Major revision
On 24 Feb, 2021
Review #2 received
Received 09 Feb, 2021
Reviewer #2 agreed
On 17 Jan, 2021
Review #1 received
Received 21 Dec, 2020
Editor assigned
On 30 Nov, 2020
Reviewers invited
Invitations sent on 30 Nov, 2020
Reviewer #1 agreed
On 30 Nov, 2020
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On 22 Nov, 2020
Editor invited
On 17 Nov, 2020
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On 09 Nov, 2020
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A new preprint design is coming!
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See the published version of this preprint at BMC Plant Biology.
This is a preprint, a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Learn more about In Review
Research article
Stefanie J. Mueller-Schuessele
University of Bonn
Corresponding Author
ORCiD: https://orcid.org/0000-0003-4061-1175
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
Peer Review Timeline
CURRENT STATUS: Published
View the published article at BMC Plant Biology.
Version 1
Posted 01 Dec, 2020
No community comments so far
Editorial decision: Major revision
On 24 Feb, 2021
Review #2 received
Received 09 Feb, 2021
Reviewer #2 agreed
On 17 Jan, 2021
Review #1 received
Received 21 Dec, 2020
Editor assigned
On 30 Nov, 2020
Reviewers invited
Invitations sent on 30 Nov, 2020
Reviewer #1 agreed
On 30 Nov, 2020
Submission checks complete
On 22 Nov, 2020
Editor invited
On 17 Nov, 2020
First submitted
On 09 Nov, 2020
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
License:
This work is licensed under a CC BY 4.0 License. Read Full License
View the published article at BMC Plant Biology.
Background: Flexibility of plant metabolism is supported by redox regulation of enzymes via posttranslational modification of cysteine residues, especially in plastids. Here, the redox states of cysteine residues are partly coupled to the thioredoxin system and partly to the glutathione pool for reduction. Moreover, several plastid enzymes involved in reactive oxygen species (ROS) scavenging and damage repair draw electrons from glutathione. In addition, cysteine residues can be post-translationally modified by forming a disulfide with glutathione (S-glutathionylation), which protects thiol groups from further oxidation and can influence protein activity. However, the evolution of the plastid glutathione-dependent redox network in land plants and the conservation of cysteine residues undergoing S-glutathionylation is largely unclear.
Results: We analysed the genomes of nine representative model species from streptophyte algae to angiosperms and find that the components of the plastid glutathione-dependent redox network are largely conserved, except for lambda- and the closely related iota-glutathione S-transferases. Screening the literature for target thiols of S-glutathionylation, we find that 151 plastid proteins have been identified as glutathionylation targets, while the exact cysteine residue is only known for 17% (26 proteins), with one or multiple sites per protein, resulting in 37 known S-glutathionylation sites for plastids. However, 38% (14) of the known sites were completely conserved in model species from green algae to flowering plants, with 22% (8) on non-catalytic cysteines. Variable conservation of the remaining sites indicates independent gains and losses of cysteines at the same position during land plant evolution.
Conclusions: We conclude that the glutathione dependent redox network in plastids is highly conserved in streptophytes with some variability in scavenging and damage repair enzymes. Our analysis of cysteine conservation suggests that S-glutathionylation in plastids plays an important and yet under-investigated role in redox regulation and stress response.
Figure 1
Figure 1
Figure 2
Figure 2
Figure 3
Figure 3
Figure 4
Figure 4
This is a list of supplementary files associated with this preprint. Click to download.
- Additionalfile10alignmentssites.docx
Word-file (DOCX) containing all alignments used to assess conservation of known S-glutathionylation sites on plastid proteins in fasta format
- Additionalfile10alignmentssites.docx
Word-file (DOCX) containing all alignments used to assess conservation of known S-glutathionylation sites on plastid proteins in fasta format
- Additionalfile11alignmentstrees.docx
Word-file (DOCX) containing all alignments used to build phylogenetic trees in FASTA format.
- Additionalfile11alignmentstrees.docx
Word-file (DOCX) containing all alignments used to build phylogenetic trees in FASTA format.
- Additionalfile12PhylogenetictreesML.docx
Word-file (DOCX) containing phylogenetic trees generated with alternative method (Maximum Likelihood)
- Additionalfile12PhylogenetictreesML.docx
Word-file (DOCX) containing phylogenetic trees generated with alternative method (Maximum Likelihood)
- Additionalfile1TableS1201105.xlsx
Table S1 containing protein model information and targeting predictions (XLSX)
- Additionalfile1TableS1201105.xlsx
Table S1 containing protein model information and targeting predictions (XLSX)
- Additionalfile2DHAR201106.pdf
Phylogenetic tree of DHAR (PDF)
- Additionalfile2DHAR201106.pdf
Phylogenetic tree of DHAR (PDF)
- Additionalfile3GSTLI201106.pdf
Phylogenetic tree of GSTI and GSTL (PDF)
- Additionalfile3GSTLI201106.pdf
Phylogenetic tree of GSTI and GSTL (PDF)
- Additionalfile4MSRB201109.pdf
Phylogenetic tree of MSRB (PDF)
- Additionalfile4MSRB201109.pdf
Phylogenetic tree of MSRB (PDF)
- Additionalfile5PRXIIE200804.pdf
Phylogenetic tree of PRXIIE (PDF)
- Additionalfile5PRXIIE200804.pdf
Phylogenetic tree of PRXIIE (PDF)
- Additionalfile6GRXclass1201106.pdf
Phylogenetic tree of PRXIIE (PDF)
- Additionalfile6GRXclass1201106.pdf
Phylogenetic tree of PRXIIE (PDF)
- Additionalfile7GRXS14S16201106.pdf
Phylogenetic tree of GRXS14 and GRXS16 (PDF)
- Additionalfile7GRXS14S16201106.pdf
Phylogenetic tree of GRXS14 and GRXS16 (PDF)
- Additionalfile8GR200804.pdf
Phylogenetic tree of GR (PDF)
- Additionalfile8GR200804.pdf
Phylogenetic tree of GR (PDF)
- Additionalfile9TableS2200908.xlsx
Table S2 (XLSX) Lists of S-glutathionylation sites and organisms
- Additionalfile9TableS2200908.xlsx
Table S2 (XLSX) Lists of S-glutathionylation sites and organisms
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