Cooperative Protein Folding by Two Protein Thiol Disulfide Oxidoreductases and ERO1 in Soybean

Matsusaki, Motonori; Okuda, Aya; Masuda, Taro; Koishihara, Katsunori; Mita, Ryuta; Iwasaki, Kensuke; Hara, Kumiko; Naruo, Yurika; Hirose, Akiho; Tsuchi, Yuichiro; Urade, Reiko

doi:10.1104/pp.15.01781

Cited by 28 publications

(50 citation statements)

References 54 publications

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“…a). In line with this assumption, soybean ERO1 was shown to oxidize multiple PDIs (PDIL1, S1, S2 and M but not L2) unlike mammalian EROs which have a high specificity towards the sole PDI (Matsusaki et al ., ). However, these four PDIs possess quite similar RNAse A oxidative refolding activity and have the capacity to associate with precursors of glycinins as shown by imunoprecipitation experiments, hence exhibiting no substrate preference in this case (Wadahama et al ., , ; Kamauchi et al ., ).…”

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

confidence: 97%

“…b). The latter model is indeed supported by a consecutive transfer of electrons from substrate proteins to soybean PDI‐L2 and then via PDI‐M to ERO (Matsusaki et al ., ). The electron transfer in this case occurs not linearly, but rather involves the different subdomains of both PDIs (Fig.…”

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

confidence: 98%

“…The formed disulfide bond is transferred sequentially from a′ of PDI‐M to the a domain of PDI‐M (II), either the a or a′ domain of PDI‐L2 (III), and the substrate (IV). Thiol–disulfide exchange between the redox‐active domains a and a′ of PDI‐L2 is unclear (Matsusaki et al ., ). Red dots indicate thiol groups participating in the disulfide transfer reactions.…”

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

confidence: 99%

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

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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 Thementioning

confidence: 97%

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

confidence: 98%

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

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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“…In this study, we found that GmPDIL7, an ER membrane‐bound protein, was rapidly oxidized by GmERO1a, which is also an ER membrane protein . Even though GmPDIL7 has only one active center, its oxidation activity was similar to the activity of other PDI family proteins that have two active centers.…”

Section: Resultsmentioning

confidence: 62%

“…The oxidative refolding of denatured RNase A by GmPDIM in the presence of GmERO1a is reportedly synergistically accelerated by GmPDIL‐2 (Fig. F) . The coexistence of GmPDIL7 with GmPDIM and GmPDIL‐2 shortened the lag time, but caused a significant decrease in the refolding rate (Fig.…”

Section: Resultsmentioning

confidence: 86%

Identification and characterization of GmPDIL7, a soybean ER membrane‐bound protein disulfide isomerase family protein

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Fortification of Bread With Soy Protein to Normalize Serum Cholesterol and Triacylglycerol Levels

Urade

2019

Flour and Breads and Their Fortification in Health and Disease Prevention

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Cooperative Protein Folding by Two Protein Thiol Disulfide Oxidoreductases and ERO1 in Soybean

Cited by 28 publications

References 54 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 and characterization of GmPDIL7, a soybean ER membrane‐bound protein disulfide isomerase family protein

Fortification of Bread With Soy Protein to Normalize Serum Cholesterol and Triacylglycerol Levels

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