On the Quaternary Assembly of Spinach Chloroplast Thioredoxin m

Capitani, Guido; Schürmann, Peter

doi:10.1023/b:pres.0000017197.03467.81

Cited by 6 publications

(4 citation statements)

References 19 publications

(33 reference statements)

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“…Nicotiana tabacum Trxs were modelled by using the protein structure homology-modelling server, SWISS-MODEL (Arnold et al , 2006; Kiefer et al , 2009), with the representative structure of Trxs from Spinacea oleracea (Protein Data Bank entry 1F9M for Trx f and 1FB6A for Trx m; Capitani and Schurmann, 2004) as templates. The schematic representations and surfaces were obtained by using the PyMOL program.…”

Section: Methodsmentioning

confidence: 99%

Chaperone-like properties of tobacco plastid thioredoxins f and m

Sanz-Barrio

Millán

Carballeda

et al. 2011

Journal of Experimental Botany

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Thioredoxins (Trxs) are ubiquitous disulphide reductases that play important roles in the redox regulation of many cellular processes. However, some redox-independent functions, such as chaperone activity, have also been attributed to Trxs in recent years. The focus of our study is on the putative chaperone function of the well-described plastid Trxs f and m. To that end, the cDNA of both Trxs, designated as NtTrxf and NtTrxm, was isolated from Nicotiana tabacum plants. It was found that bacterially expressed tobacco Trx f and Trx m, in addition to their disulphide reductase activity, possessed chaperone-like properties. In vitro, Trx f and Trx m could both facilitate the reactivation of the cysteine-free form of chemically denatured glucose-6 phosphate dehydrogenase (foldase chaperone activity) and prevent heat-induced malate dehydrogenase aggregation (holdase chaperone activity). Our results led us to infer that the disulphide reductase and foldase chaperone functions prevail when the proteins occur as monomers and the well-conserved non-active cysteine present in Trx f is critical for both functions. By contrast, the holdase chaperone activity of both Trxs depended on their oligomeric status: the proteins were functional only when they were associated with high molecular mass protein complexes. Because the oligomeric status of both Trxs was induced by salt and temperature, our data suggest that plastid Trxs could operate as molecular holdase chaperones upon oxidative stress, acting as a type of small stress protein.

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Section: Methodsmentioning

confidence: 99%

Chaperone-like properties of tobacco plastid thioredoxins f and m

Sanz-Barrio

Millán

Carballeda

et al. 2011

Journal of Experimental Botany

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“…The interaction surface is distant from the redox site and may rather serve to scaffold TRXz‐containing complexes with internal twofold symmetries. Other TRX quaternary states were tested in the past and TRX proved monomeric (Capitani and Schurmann, 2004; Gronenborn et al. , 1999) in the reduced state (Weichsel et al.…”

Section: Discussionmentioning

confidence: 99%

“…Other TRX quaternary states were tested in the past and TRX proved monomeric (Capitani and Schurmann, 2004;Gronenborn et al, 1999) in the reduced state (Weichsel et al, 1996).…”

Section: Crtrxz Evolved Distinct Featuresmentioning

confidence: 99%

Crystal structure of chloroplastic thioredoxin z defines a type‐specific target recognition

et al. 2021

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Summary Thioredoxins (TRXs) are ubiquitous disulfide oxidoreductases structured according to a highly conserved fold. TRXs are involved in a myriad of different processes through a common chemical mechanism. Plant TRXs evolved into seven types with diverse subcellular localization and distinct protein target selectivity. Five TRX types coexist in the chloroplast, with yet scarcely described specificities. We solved the crystal structure of a chloroplastic z‐type TRX, revealing a conserved TRX fold with an original electrostatic surface potential surrounding the redox site. This recognition surface is distinct from all other known TRX types from plant and non‐plant sources and is exclusively conserved in plant z‐type TRXs. We show that this electronegative surface endows thioredoxin z (TRXz) with a capacity to activate the photosynthetic Calvin–Benson cycle enzyme phosphoribulokinase. The distinct electronegative surface of TRXz thereby extends the repertoire of TRX–target recognitions.

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“…The interaction surface is distant from the redox site and may rather serve to scaffold TRXz-containing complexes with internal two-fold symmetries. Other TRX quaternary states were tested in the past and proved monomeric [87, 88] in reduced state [89].…”

Section: Discussionmentioning

confidence: 99%

Crystal structure of chloroplastic thioredoxin z defines a novel type-specific target recognition

Moigne

Gurrieri

Crozet

et al. 2020

Preprint

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Thioredoxins (TRXs) are ubiquitous disulfide oxidoreductases structured according to a highly conserved fold. TRXs are involved in a myriad of different processes through a common chemical mechanism. Plant thioredoxins evolved into seven types with diverse subcellular localization and distinct protein targets selectivity. Five TRX types coexist in the chloroplast, with yet scarcely described specificities. We solved the first crystal structure of a chloroplastic z-type TRX, revealing a conserved TRX fold with an original electrostatic surface potential surrounding the redox site. This recognition surface is distinct from all other known TRX types from plant and non-plant sources and is exclusively conserved in plant z-type TRXs. We show that this electronegative surface endows TRXz with a capacity to activate the photosynthetic Calvin-Benson cycle enzyme phosphoribulokinase. TRXz distinct electronegative surface thereby extends the repertoire of TRX-target recognitions.

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On the Quaternary Assembly of Spinach Chloroplast Thioredoxin m

Cited by 6 publications

References 19 publications

Chaperone-like properties of tobacco plastid thioredoxins f and m

Chaperone-like properties of tobacco plastid thioredoxins f and m

Crystal structure of chloroplastic thioredoxin z defines a type‐specific target recognition

Crystal structure of chloroplastic thioredoxin z defines a novel type-specific target recognition

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