Allosteric Control of βII-Tryptase by a Redox Active Disulfide Bond

Cook, Kristina M.; McNeil, H. Patrick; Hogg, Philip J.

doi:10.1074/jbc.m113.523506

Cited by 22 publications

(19 citation statements)

References 61 publications

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“…Considering the light-, temperature-, and droughtsensitive processes of photosynthesis and pigment biosynthesis in the chloroplast, redox-dependent regulation is adequate for rapidly modulating protein activity, folding, and stability (Cook et al, 2013;Kang and Wang, 2016;Nikkanen et al, 2016). Several enzymes of TBS are redox controlled by different reductants (Ikegami et al, 2007;Luo et al, 2012;Pérez-Ruiz et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

Thioredoxin and NADPH-Dependent Thioredoxin Reductase C Regulation of Tetrapyrrole Biosynthesis

Wang

et al. 2017

Plant Physiol.

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In chloroplasts, thioredoxin (TRX) isoforms and NADPH-dependent thioredoxin reductase C (NTRC) act as redox regulatory factors involved in multiple plastid biogenesis and metabolic processes. To date, less is known about the functional coordination between TRXs and NTRC in chlorophyll biosynthesis. In this study, we aimed to explore the potential functions of TRX m and NTRC in the regulation of the tetrapyrrole biosynthesis (TBS) pathway. Silencing of three genes, TRX m1, TRX m2, and TRX m4 (TRX ms), led to pale-green leaves, a significantly reduced 5-aminolevulinic acid (ALA)-synthesizing capacity, and reduced accumulation of chlorophyll and its metabolic intermediates in Arabidopsis (Arabidopsis thaliana). The contents of ALA dehydratase, protoporphyrinogen IX oxidase, the I subunit of Mg-chelatase, Mg-protoporphyrin IX methyltransferase (CHLM), and NADPH-protochlorophyllide oxidoreductase were decreased in triple TRX m-silenced seedlings compared with the wild type, although the transcript levels of the corresponding genes were not altered significantly. Protein-protein interaction analyses revealed a physical interaction between the TRX m isoforms and CHLM. 4-Acetoamido-4-maleimidylstilbene-2,2-disulfonate labeling showed the regulatory impact of TRX ms on the CHLM redox status. Since CHLM also is regulated by NTRC , we assessed the concurrent functions of TRX m and NTRC in the control of CHLM. Combined deficiencies of three TRX m isoforms and NTRC led to a cumulative decrease in leaf pigmentation, TBS intermediate contents, ALA synthesis rate, and CHLM activity. We discuss the coordinated roles of TRX m and NTRC in the redox control of CHLM stability with its corollary activity in the TBS pathway.

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Section: Discussionmentioning

confidence: 99%

Thioredoxin and NADPH-Dependent Thioredoxin Reductase C Regulation of Tetrapyrrole Biosynthesis

Wang

et al. 2017

Plant Physiol.

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“…The bII-tryptase Cys220-Cys248 disulfide bond exists in oxidized and reduced states in the secreted enzyme and the bond is reduced by thioredoxin in the isolated enzyme. 36 The oxidized and reduced isoforms have different specificity and catalytic efficiency for hydrolysis of substrates.…”

Section: Control Of Blood Proteins By Disulfide Bond Cleavage 2003mentioning

confidence: 99%

“…36,41,42,97 The approach is based on the principle that an allosteric disulfide will exist in equilibrium between reduced and oxidized states in a blood protein, such as observed in angiotensinogen, b2-glycoprotein I, and plasminogen. The technique measures the proportion of reduced and oxidized protein using different thiol alkylating agents.…”

Section: Experimental Approachmentioning

confidence: 99%

Control of blood proteins by functional disulfide bonds

Butera

Cook

Chiu

et al. 2014

Blood

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Most proteins in nature are chemically modified after they are made to control how, when, and where they function. The 3 core features of proteins are posttranslationally modified: amino acid side chains can be modified, peptide bonds can be cleaved or isomerized, and disulfide bonds can be cleaved. Cleavage of peptide bonds is a major mechanism of protein control in the circulation, as exemplified by activation of the blood coagulation and complement zymogens. Cleavage of disulfide bonds is emerging as another important mechanism of protein control in the circulation. Recent advances in our understanding of control of soluble blood proteins and blood cell receptors by functional disulfide bonds is discussed as is how these bonds are being identified and studied.

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“…This scenario has parallels with the regulation of the mast cell serine protease, ␤II-tryptase (28). No endogenous inhibitors of ␤II-tryptase have been identified, and the secreted enzyme is not restricted to specific extracellular environments.…”

Section: Discussionmentioning

confidence: 99%

“…The MetAP2 disulfide has a higher redox potential than the thioredoxin catalytic disulfide, Ϫ264 versus Ϫ270 mV (23), and the rate of the reaction is very efficient. For instance, thioredoxin reduces the MetAP2 disulfide 46 times faster than the ␤II-tryptase allosteric disulfide bond (16,180 versus 350 M Ϫ1 s Ϫ1 ) (28). It is interesting that newly synthesized thioredoxin itself is a substrate for MetAP2 (5).…”

Section: Discussionmentioning

confidence: 99%

Redox Regulation of Methionine Aminopeptidase 2 Activity

Chiu

Wong

Hogg

2014

Journal of Biological Chemistry

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Background:The N-terminal methionine in new eukaryote proteins is removed by methionine aminopeptidases, but how these enzymes are regulated is not known. Results: Methionine aminopeptidase 2 contains a single disulfide bond that exists in oxidized and reduced states and influences enzyme function. Conclusion: MetAP2 is regulated by an allosteric disulfide bond. Significance: This has implications for MetAP2 substrate proteins and other similar enzymes.

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Allosteric Control of βII-Tryptase by a Redox Active Disulfide Bond

Cited by 22 publications

References 61 publications

Thioredoxin and NADPH-Dependent Thioredoxin Reductase C Regulation of Tetrapyrrole Biosynthesis

Thioredoxin and NADPH-Dependent Thioredoxin Reductase C Regulation of Tetrapyrrole Biosynthesis

Control of blood proteins by functional disulfide bonds

Redox Regulation of Methionine Aminopeptidase 2 Activity

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