Defining the plant disulfide proteome

Lee, Kyung‐Hee; Lee, Jung Hwa; Kim, Young‐Min; Bae, Dong-Won; Kang, Kyu Young; Yoon, Sung Chul; Lim, Dongbin

doi:10.1002/elps.200305677

Cited by 74 publications

(59 citation statements)

References 52 publications

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“…4]. Affinity purification and identification of cellular disulfide-containing proteins by mass spectrometry (SI Table 1) reveal nine proteins, seven of which are cell-surface membrane proteins known to contain disulfides, which is consistent with studies in plants (11) and E. coli (12) reporting that, under normal growth conditions, most proteins containing disulfides are secreted or membrane-bound. Upon treatment with the mitochondrial uncoupler carbonylcyanide m-chlorophenylhydrazone (CCCP), the overall signal decreased (Fig.…”

Section: Resultssupporting

confidence: 77%

Regulation of the protein disulfide proteome by mitochondria in mammalian cells

Yang

Song

Loscalzo

2007

Proc. Natl. Acad. Sci. U.S.A.

119

107

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The majority of protein disulfides in cells is considered an important inert structural, rather than a dynamic regulatory, determinant of protein function. Here, we show that some disulfides in proteins also are regulated by cell redox status with functional consequences. We find that reactive oxygen species (ROS) produced by mitochondria are actively used by cells to facilitate cell-surface protein disulfide formation, as well as folding and transport, in mammalian cells. Inhibition of mitochondrial ROS production suppresses protein disulfide formation and induces reductive stress, leading to dysfunction and retention (possibly in the Golgi, in part) of a group of cell-surface disulfide-containing proteins. Sparsely cultured cells produce less ROS than confluent cells do, which leads to decreased disulfide formation and decreased activity of a subgroup of disulfide-containing cell-surface receptors. These data support the concept of two subproteomes comprising the disulfide proteome, a structural group and a redox-sensitive regulatory group, with the latter having direct functional consequences for the cell.

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Section: Resultssupporting

confidence: 77%

Regulation of the protein disulfide proteome by mitochondria in mammalian cells

Yang

Song

Loscalzo

2007

Proc. Natl. Acad. Sci. U.S.A.

119

107

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“…Yano et al used monobromobimane to label free thiols in proteins reduced by Trx that were resolved via two-dimensional gel electrophoresis and identified five Trx targets in peanut seeds (26). The Trx affinity technique was subsequently developed to identify Trx targets in diverse cell types, including spinach (27)(28)(29)(30)(31), Arabidopsis (32)(33)(34)(35), Escherichia coli (36,37), wheat seeds (38,39), Synechocystis (40 -42), and HeLa cells (16,43). The most successful of these studies identified up to 80 putative Trx targets (37).…”

Section: Discussionmentioning

confidence: 99%

“…More recently, we used the isotope-coded affinity tag approach to identify over 70 targets of Trx1 transnitrosylation and 50 targets of Trx1-mediated denitrosylation (43). Although a Trx mutant has been used to identify Trx targets in non-mammalian cells (25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35)(36)(37)(38)(39)(40)(41)(42)44), its application in the identification of mammalian targets has been rare, presumably because of the presence of highly abundant cytosolic targets in the total cell lysates, such as Prx1, that compete for a limited number of binding sites on the Trx1 C35S mutant. This is the first report demonstrating that an nTrx1 C35S mutant can be used to identify novel Trx1 targets in the nucleus of mammalian cells.…”

Section: Discussionmentioning

confidence: 99%

Identification of Novel Nuclear Targets of Human Thioredoxin 1

Jain

et al. 2014

Molecular & Cellular Proteomics

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The dysregulation of protein oxidative post-translational modifications has been implicated in stress-related diseases. Trx1 is a key reductase that reduces specific disulfide bonds and other cysteine post-translational modifications. Although commonly in the cytoplasm, Trx1 can also modulate transcription in the nucleus. However, few Trx1 nuclear targets have been identified because of the low Trx1 abundance in the nucleus. Here, we report the large-scale proteomics identification of nuclear Trx1 targets in human neuroblastoma cells using an affinity capture strategy wherein a Trx1C35S mutant is expressed. The wild-type Trx1 contains a conserved C32XXC35 motif, and the C32 thiol initiates the reduction of a target disulfide bond by forming an intermolecular disulfide with one of the oxidized target cysteines, resulting in a transient Trx1-target protein complex. The reduction is rapidly consummated by the donation of a C35 proton to the target molecule, forming a Trx1 C32-C35 disulfide, and results in the concurrent release of the target protein containing reduced thiols. By introducing a point mutation (C35 to S35) in Trx1, we ablated the rapid dissociation of Trx1 from its reduction targets, thereby allowing the identification of 45 putative nuclear Trx1 targets. Unexpectedly, we found that PSIP1, also known as LEDGF, was sensitive to both oxidation and Trx1 reduction at Cys 204. LEDGF is a transcription activator that is vital for regulating cell survival during HIV-1 infection. Overall, this study suggests that Trx1 may play a broader role than previously believed that might include regulating transcription, RNA processing, and nuclear pore function in human cells. Molecular

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“…Such a mode of activation, in which an enzyme of the lumen is rendered active when oxidized in the light, contrasts with the mechanism functional in the stroma. The relation of electron transfer proteins of the lumen (36) [HCF164 (37), thylakoid luminal protein (38), oxygen-evolving enhancer protein (39), and CcdA (40)] to the scheme depicted in Fig. 5 …”

Section: Fkbp13 Is a Target For Reduction By Thioredoxinmentioning

confidence: 99%

Structural analysis uncovers a role for redox in regulating FKBP13, an immunophilin of the chloroplast thylakoid lumen

Gopalan

He²,

Balmer³

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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Change in redox status has long been known to link light to the posttranslational regulation of chloroplast enzymes. So far, studies have been conducted primarily with thioredoxin-linked members of the stroma that function in a broad array of biosynthetic and degradatory processes. Consequently, little is known about the role of redox in regulating the growing number of enzymes found to occur in the lumen, the site of oxygen evolution in thylakoid membranes. To help fill this gap, we have studied AtFKBP13, an FKBP-type immunophilin earlier shown to interact with a redoxactive protein of the lumen, and found the enzyme to contain a pair of disulfide bonds in x-ray structural studies. These disulfides, which in protein mutagenesis experiments were shown to be essential for the associated peptidyl-prolyl isomerase activity, are unique to chloroplast FKBPs and are absent in animal and yeast counterparts. Both disulfide bonds were redox-active and were reduced by thioredoxin from either chloroplast or bacterial sources in a reaction that led to loss of enzyme activity. The results suggest a previously unrecognized paradigm for redox regulation in chloroplasts in which activation by light is achieved in concert with oxygen evolution by the oxidation of sulfhydryl groups (conversion of SH to SOS). Such a mechanism, occurring in the thylakoid lumen, is in direct contrast to regulation of enzymes in the stroma, where reduction of disulfides targeted by thioredoxin (SOS converted to SH) leads to an increase in activity in the light.

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Defining the plant disulfide proteome

Cited by 74 publications

References 52 publications

Regulation of the protein disulfide proteome by mitochondria in mammalian cells

Regulation of the protein disulfide proteome by mitochondria in mammalian cells

Identification of Novel Nuclear Targets of Human Thioredoxin 1

Structural analysis uncovers a role for redox in regulating FKBP13, an immunophilin of the chloroplast thylakoid lumen

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