FK506-Binding Protein 22 from a Psychrophilic Bacterium, a Cold Shock-Inducible Peptidyl Prolyl Isomerase with the Ability to Assist in Protein Folding

Budiman, Cahyo; Koga, Yuichi; Takano, Kazufumi; Kanaya, Shigenori

doi:10.3390/ijms12085261

Cited by 28 publications

(16 citation statements)

References 70 publications

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“…However, unknown protein 18 and unnamed protein product could not be identified, probably these are not yet reported. PPIases identified in this study are ubiquitous proteins, mediating protein folding in cold stress (Budiman et al, 2011). Additionally, ROC4 (only cyclophilin in the stroma of the chloroplast) is shown to have PPIases activity and is involved in the repair of photo-damaged PSII in A. thaliana (Cai et al, 2008).…”

Section: Discussionmentioning

confidence: 85%

RuBisCO depletion improved proteome coverage of cold responsive S-nitrosylated targets in Brassica juncea

Sehrawat¹,

Abat²,

Deswal³

2013

Front. Plant Sci.

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Although in the last few years good number of S-nitrosylated proteins are identified but information on endogenous targets is still limiting. Therefore, an attempt is made to decipher NO signaling in cold treated Brassica juncea seedlings. Treatment of seedlings with substrate, cofactor and inhibitor of Nitric-oxide synthase and nitrate reductase (NR), indicated NR mediated NO biosynthesis in cold. Analysis of the in vivo thiols showed depletion of low molecular weight thiols and enhancement of available protein thiols, suggesting redox changes. To have a detailed view, S-nitrosylation analysis was done using biotin switch technique (BST) and avidin-affinity chromatography. Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is S-nitrosylated and therefore, is identified as target repeatedly due to its abundance. It also competes out low abundant proteins which are important NO signaling components. Therefore, RuBisCO was removed (over 80%) using immunoaffinity purification. Purified S-nitrosylated RuBisCO depleted proteins were resolved on 2-D gel as 110 spots, including 13 new, which were absent in the crude S-nitrosoproteome. These were identified by nLC-MS/MS as thioredoxin, fructose biphosphate aldolase class I, myrosinase, salt responsive proteins, peptidyl-prolyl cis-trans isomerase and malate dehydrogenase. Cold showed differential S-nitrosylation of 15 spots, enhanced superoxide dismutase activity (via S-nitrosylation) and promoted the detoxification of superoxide radicals. Increased S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase sedoheptulose-biphosphatase, and fructose biphosphate aldolase, indicated regulation of Calvin cycle by S-nitrosylation. The results showed that RuBisCO depletion improved proteome coverage and provided clues for NO signaling in cold.

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Section: Discussionmentioning

confidence: 85%

RuBisCO depletion improved proteome coverage of cold responsive S-nitrosylated targets in Brassica juncea

Sehrawat¹,

Abat²,

Deswal³

2013

Front. Plant Sci.

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“…Different members of cyclophilin subfamily were directly linked to multiple stresses. In this sense, Budiman et al ( 2011 ) proposed that foldase and chaperone activities of PPIases are the main requirements with which to overcome the cold-stress problem in microorganisms caused by protein folding.…”

Section: Discussionmentioning

confidence: 99%

Low Temperature and Short-Term High-CO2 Treatment in Postharvest Storage of Table Grapes at Two Maturity Stages: Effects on Transcriptome Profiling

et al. 2016

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Table grapes (Vitis vinifera cv. Cardinal) are highly perishable and their quality deteriorates during postharvest storage at low temperature mainly because of sensitivity to fungal decay and senescence of rachis. The application of a 3-day CO2 treatment (20 kPa CO2 + 20 kPa O2 + 60 kPa N2) at 0°C reduced total decay and retained fruit quality in early and late-harvested table grapes during postharvest storage. In order to study the transcriptional responsiveness of table grapes to low temperature and high CO2 levels in the first stage of storage and how the maturity stage affect these changes, we have performed a comparative large-scale transcriptional analysis using the custom-made GrapeGen GeneChip®. In the first stage of storage, low temperature led to a significantly intense change in grape skin transcriptome irrespective of fruit maturity, although there were different changes within each stage. In the case of CO2 treated samples, in comparison to fruit at time zero, only slight differences were observed. Functional enrichment analysis revealed that major modifications in the transcriptome profile of early- and late-harvested grapes stored at 0°C are linked to biotic and abiotic stress-responsive terms. However, in both cases there is a specific reprogramming of the transcriptome during the first stage of storage at 0°C in order to withstand the cold stress. Thus, genes involved in gluconeogenesis, photosynthesis, mRNA translation and lipid transport were up-regulated in the case of early-harvested grapes, and genes related to protein folding stability and intracellular membrane trafficking in late-harvested grapes. The beneficial effect of high CO2 treatment maintaining table grape quality seems to be an active process requiring the induction of several transcription factors and kinases in early-harvested grapes, and the activation of processes associated to the maintenance of energy in late-harvested grapes.

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“…It has been reported that the rate of cis/trans proline isomerization at low temperature is much slower than at higher temperatures, and consequently, folding of cis proline-containing proteins is the rate-limiting step for bacterial growth in cold environments (46). Thus, it was interesting to determine if the Brucella ⌬cypAB mutant has a reduced ability to grow at lower temperatures.…”

Section: Resultsmentioning

confidence: 99%

Intracellularly Induced Cyclophilins Play an Important Role in Stress Adaptation and Virulence of Brucella abortus

et al. 2013

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bBrucella is an intracellular bacterial pathogen that causes the worldwide zoonotic disease brucellosis. Brucella virulence relies on its ability to transition to an intracellular lifestyle within host cells. Thus, this pathogen must sense its intracellular localization and then reprogram gene expression for survival within the host cell. A comparative proteomic investigation was performed to identify differentially expressed proteins potentially relevant for Brucella intracellular adaptation. Two proteins identified as cyclophilins (CypA and CypB) were overexpressed in the intracellular environment of the host cell in comparison to laboratorygrown Brucella. To define the potential role of cyclophilins in Brucella virulence, a double-deletion mutant was constructed and its resulting phenotype was characterized. The Brucella abortus ⌬cypAB mutant displayed increased sensitivity to environmental stressors, such as oxidative stress, pH, and detergents. In addition, the B. abortus ⌬cypAB mutant strain had a reduced growth rate at lower temperature, a phenotype associated with defective expression of cyclophilins in other microorganisms. The B. abortus ⌬cypAB mutant also displays reduced virulence in BALB/c mice and defective intracellular survival in HeLa cells. These findings suggest that cyclophilins are important for Brucella virulence and survival in the host cells. C yclophilins (Cyps) are folding helper enzymes that belong to the enzyme class of peptidyl prolyl cis/trans isomerases (PPIases; EC 5.2.1.8). In addition to cyclophilins, PPIases also includes FK506-binding proteins (FKBPs) and parvulins. These three families of proteins that have no sequence or structural homology can be distinguished by being inhibited by the immunosuppressive compounds cyclosporine, FK506, and rapamycin, respectively (1, 2). PPIases catalyze the cis/trans isomerization of peptidyl prolyl bonds. This reaction requires free energy and as a consequence is a slow process at lower temperatures, being the rate-limiting step in protein folding (3). PPIases are thought to be important for the correct folding of nascent proteins as well as their refolding (4-6). It is postulated that conformational isomerization by PPIases controls the activity of target proteins, regulating the interaction with other partner proteins to form complexes (3, 7).Cyclophilins are evolutionary conserved and have been found in all organisms analyzed to date, with the exception of Mycoplasma genitalium and some members of the Archaea (8). They are ubiquitously distributed proteins and like the other PPIases are critical for cell adaptation under stress conditions (9). Cyclophilins have been reported to be involved in several processes, such as adaptation to environmental stress, cell cycle control, signal transduction, and transcriptional regulation (8, 10-12). In addition, they have been implicated in the virulence of fungal and parasitic pathogens (13-17). Recent reports have shown the involvement of PPIases in stress tolerance and pathogenesis of bacteria, su...

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FK506-Binding Protein 22 from a Psychrophilic Bacterium, a Cold Shock-Inducible Peptidyl Prolyl Isomerase with the Ability to Assist in Protein Folding

Cited by 28 publications

References 70 publications

RuBisCO depletion improved proteome coverage of cold responsive S-nitrosylated targets in Brassica juncea

RuBisCO depletion improved proteome coverage of cold responsive S-nitrosylated targets in Brassica juncea

Low Temperature and Short-Term High-CO2 Treatment in Postharvest Storage of Table Grapes at Two Maturity Stages: Effects on Transcriptome Profiling

Intracellularly Induced Cyclophilins Play an Important Role in Stress Adaptation and Virulence of Brucella abortus

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