Characterization of the oxidative protein folding activity of a unique plant oxidoreductase, Arabidopsis protein disulfide isomerase-11

Fan, Fenggui; Zhang, Yini; Wang, Shen; Han, Yong-Feng; Wang, Lei; Lu, Dongping

doi:10.1016/j.bbrc.2017.11.111

Cited by 14 publications

(20 citation statements)

References 24 publications

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“…High expression of PDIs during grain filling in the starchy endosperm of wheat suggests that these proteins play an important role in forming intramolecular disulfide bonds in seed storage proteins and are upregulated according to demand (Kimura et al ., ). The A. thaliana PDI11 with an a‐a′‐D architecture and belonging to the plant‐specific PDI‐S class has recently been demonstrated to exhibit oxidoreductase activity in vitro at the expense of glutathione (Fan et al ., ). Genetic evidence suggests that null‐mutants deficient in PDI‐S are impaired in plant growth under reducing conditions and display defects in pollen tube guidance (Wang et al ., ; Fan et al ., ).…”

Section: Formation and Isomerization Of Disulfides In The Er And The mentioning

confidence: 99%

“…The A. thaliana PDI11 with an a‐a′‐D architecture and belonging to the plant‐specific PDI‐S class has recently been demonstrated to exhibit oxidoreductase activity in vitro at the expense of glutathione (Fan et al ., ). Genetic evidence suggests that null‐mutants deficient in PDI‐S are impaired in plant growth under reducing conditions and display defects in pollen tube guidance (Wang et al ., ; Fan et al ., ). The latter phenotype might be explained by impaired disulfide formation in defensin‐like polypeptides that are secreted from synergid cells and act as pollen tube attractants (Okuda et al ., ; Chae & Lord, ).…”

Section: Formation and Isomerization Of Disulfides In The Er And The mentioning

confidence: 99%

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Oxidative protein folding: state‐of‐the‐art and current avenues of research in plants

2018

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Contents Summary I. Introduction II. Formation and isomerization of disulfides in the ER and the Golgi apparatus III. The disulfide relay in the mitochondrial intermembrane space: why are plants different? IV. Disulfide bond formation on luminal proteins in thylakoids V. Conclusion Acknowledgements References SUMMARY: Disulfide bonds are post-translational modifications crucial for the structure and function of thousands of proteins. Their formation and isomerization, referred to as oxidative folding, require specific protein machineries found in oxidizing subcellular compartments, namely the endoplasmic reticulum and the associated endomembrane system, the intermembrane space of mitochondria and the thylakoid lumen of chloroplasts. At least one protein component is required for transferring electrons from substrate proteins to an acceptor that is usually molecular oxygen. For oxidation reactions, incoming reduced substrates are oxidized by thiol-oxidoreductase proteins (or domains in case of chimeric proteins), which are usually themselves oxidized by a single thiol oxidase, the enzyme generating disulfide bonds de novo. By contrast, the description of the molecular actors and pathways involved in proofreading and isomerization of misfolded proteins, which require a tightly controlled redox balance, lags behind. Herein we provide a general overview of the knowledge acquired on the systems responsible for oxidative protein folding in photosynthetic organisms, highlighting their particularities compared to other eukaryotes. Current research challenges are discussed including the importance and specificity of these oxidation systems in the context of the existence of reducing systems in the same compartments.

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Section: Formation and Isomerization Of Disulfides In The Er And The mentioning

confidence: 99%

Section: Formation and Isomerization Of Disulfides In The Er And The mentioning

confidence: 99%

Oxidative protein folding: state‐of‐the‐art and current avenues of research in plants

2018

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“…b). Nonetheless, BRI1C411A‐GFP, just like the ER‐localized protein disulfide isomerase 11 (PDI11)‐GFP‐KDEL, exhibits a reticulate fluorescence pattern, which overlaps with that of SP‐RFP‐KDEL, an ER‐localized RFP with an SP from PDI11 at the N‐terminus and an ER retention signal KDEL at the C‐terminus (Fan et al ., ; Fig. c).…”

Section: Resultsmentioning

confidence: 81%

“…Triticum aestivum AVRPPHB SUSCEPTIBLE1 ( TaPBS1 ) was subcloned into a plant expression vector fused to a red fluorescence protein (RFP) tag (Sun J. et al ., ). For SP‐RFP‐KDEL , the signal peptide (SP) of Arabidopsis protein disulfide isomerase 11 (AtPDI11; Fan et al ., ) was fused to RFP at the N‐terminus, and an ER retention signal KDEL at the C‐terminus. For PDI11‐GFP‐KDEL , PDI11 was subcloned into the plant expression vector fused to the GFP‐KDEL tag (Fan et al ., ).…”

Section: Methodsmentioning

confidence: 99%

“…For SP‐RFP‐KDEL , the signal peptide (SP) of Arabidopsis protein disulfide isomerase 11 (AtPDI11; Fan et al ., ) was fused to RFP at the N‐terminus, and an ER retention signal KDEL at the C‐terminus. For PDI11‐GFP‐KDEL , PDI11 was subcloned into the plant expression vector fused to the GFP‐KDEL tag (Fan et al ., ). BRI1 cytosolic domain ( BRI1CD ) was cloned into the modified pET‐28a vector and fused to the 6 × His and FLAG tags at its N‐terminus (Lin et al ., ; Han et al ., ).…”

Section: Methodsmentioning

confidence: 99%

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Identification of critical cysteine sites in brassinosteroid‐insensitive 1 and novel signaling regulators using a transient expression system

et al. 2019

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Summary The plant hormones brassinosteroids (BRs) modulate plant growth and development. Cysteine (Cys) residues located in the extracellular domain of a protein are of importance for protein structure by forming disulfide bonds. To date, the systematic study of the functional significance of Cys residues in BR‐insensitive 1 (BRI1) is still lacking. We used brassinolide‐induced exogenous bri1‐EMS‐Suppressor 1 (BES1) dephosphorylation in Arabidopsis thaliana protoplasts as a readout, took advantage of the dramatic decrease of BRI1 protein levels during protoplast isolation, and of the strong phosphorylation of BES1 by BR‐insensitive 2 (BIN2) in protoplasts, and developed a protoplast transient system to identify critical Cys sites in BRI1. Using this system, we identified a set of critical Cys sites in BRI1, as substitution of these Cys residues with alanine residues greatly compromised the function of BRI1. Moreover, we identified two negative regulators of BR signaling, pattern‐triggered immunity compromised RLCK1 (PCRK1) and PCRK2, that were previously known to positively regulate innate immunity signaling. This work not only provides insight into the functional importance of critical Cys residues in stabilizing the superhelical conformation of BRI1‐leucine‐rich‐repeat, but also reveals that PCRK1/2 can inversely modulate BR and plant immune signaling pathways.

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Identification of N-glycosylation sites on AtERO1 and AtERO2 using a transient expression system

Fan

Zhang

2020

Biochemical and Biophysical Research Communications

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Characterization of the oxidative protein folding activity of a unique plant oxidoreductase, Arabidopsis protein disulfide isomerase-11

Cited by 14 publications

References 24 publications

Oxidative protein folding: state‐of‐the‐art and current avenues of research in plants

Oxidative protein folding: state‐of‐the‐art and current avenues of research in plants

Identification of critical cysteine sites in brassinosteroid‐insensitive 1 and novel signaling regulators using a transient expression system

Identification of N-glycosylation sites on AtERO1 and AtERO2 using a transient expression system

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