Expression of a Gene for Cyclophilin Which Contains an Amino-Terminal Endoplasmic Reticulum-Targeting Signal

Saito, Takeshi; Niwa, Yasuo; Ashida, Hiroyuki; Tanaka, Katsunori; Kawamukai, Makoto; Matsuda, Hideyuki; Nakagawa, Tsuyoshi

doi:10.1093/oxfordjournals.pcp.a029477

Cited by 42 publications

(38 citation statements)

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“….). Studies in plants also adopted several naming strategies including those inherited from animal literature with some modifications (AtCyP40, AtCYP5, pCyPB; Luan et al, 1994b;Saito et al, 1999;Berardini et al, 2001) and a new strategy that names cyclophilins rotamase cyclophilins (ROCs; Lippuner et al, 1994;Chou and Gasser, 1997). To streamline nomenclature of cyclophilins, we suggest here that cyclophilins, like FKBPs, are named after the abbreviation CYP with prefix letters to indicate species of origin and suffix numbers to indicate M r .…”

Section: Resultsmentioning

confidence: 99%

“…Their exact location needs to be determined by further experiments. The AtCYP19-4 (CyP5) has been shown to be located in the ER by N-terminal green fluorescent protein fusion (Saito et al, 1999). This protein displayed PPIase and protein refolding activities that were sensitive to cyclosporin A (Grebe et al, 2000).…”

Section: Genomic Organization and Phylogenetic Relationship Of Arabidmentioning

confidence: 99%

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Immunophilins and Parvulins. Superfamily of Peptidyl Prolyl Isomerases in Arabidopsis

2004

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Immunophilins are defined as receptors for immunosuppressive drugs including cyclosporin A, FK506, and rapamycin. The cyclosporin A receptors are referred to as cyclophilins (CYPs) and FK506-and rapamycin-binding proteins are abbreviated as FKBPs. These two groups of proteins (collectively called immunophilins) share little sequence homology, but both have peptidyl prolyl cis/trans isomerase (PPIase) activity that is involved in protein folding processes. Studies have identified immunophilins in all organisms examined including bacteria, fungi, animals, and plants. Nevertheless, the physiological function of immunophilins is poorly understood in any organism. In this study, we have surveyed the genes encoding immunophilins in Arabidopsis genome. A total of 52 genes have been found to encode putative immunophilins, among which 23 are putative FKBPs and 29 are putative CYPs. This is by far the largest immunophilin family identified in any organism. Both FKBPs and CYPs can be classified into single domain and multiple domain members. The single domain members contain a basic catalytic domain and some of them have signal sequences for targeting to a specific organelle. The multiple domain members contain not only the catalytic domain but also defined modules that are involved in protein-protein interaction or other functions. A striking feature of immunophilins in Arabidopsis is that a large fraction of FKBPs and CYPs are localized in the chloroplast, a possible explanation for why plants have a larger immunophilin family than animals. Parvulins represent another family of PPIases that are unrelated to immunophilins in protein sequences and drug binding properties. Three parvulin genes were found in Arabidopsis genome. The expression of many immunophilin and parvulin genes is ubiquitous except for those encoding chloroplast members that are often detected only in the green tissues. The large number of genes and diversity of structure domains and cellular localization make PPIases a versatile superfamily of proteins that clearly function in many cellular processes in plants.Immunosuppressive drugs cyclosporin A (CsA), FK506, and rapamycin are used clinically in transplantation to prevent graft rejection. During the course to understand the molecular mechanisms of immunosuppression by CsA, FK506, and rapamycin, the cellular receptors of these drugs have been purified and characterized (Schreiber, 1991;Fruman et al., 1994). CsA binds to a family of receptors named cyclophilins (CyPs), and FK506 and rapamycin bind to a distinct set of receptors called FKBPs (FK506 and rapamycin-binding proteins). Cyclophilins and FKBPs are collectively referred to as immunophilins (Schreiber, 1991).The complexes formed by immunophilins and their cognate ligands are the functional modules for immunosuppression. The FKBP12-FK506 and CyPCsA complexes, but not their separate components, bind to and inhibit the activity of calcineurin, a Ca 21 , calmodulin-dependent protein phosphatase (Liu et al., 1991). Studies have demonstrated that inhib...

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Section: Resultsmentioning

confidence: 99%

Section: Genomic Organization and Phylogenetic Relationship Of Arabidmentioning

confidence: 99%

Immunophilins and Parvulins. Superfamily of Peptidyl Prolyl Isomerases in Arabidopsis

2004

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“…In another example, CYP19-2 (At2g21130) was mostly found to be expressed in young tissue and floral buds, whereas the expression analysis exhibited marked change in transcript level only in the late flowering and the senescence stage. 54 The above examples emphasize the importance of experimental verification of the in-silico data. 55 In conclusion, the cyclophilin family characterized by the presence of the PPIase domain is highly conserved in rice, Arabidopsis and the yeast genomes.…”

Section: Discussionmentioning

confidence: 99%

“…Role of a copper chaperon has also been reported in senescence previously. 53 Spatial expression of the cyclophilin proteins was found in rice during various different developmental stages, 54 while in case of Arabidopsis CYP71 (At3g44600) gene was involved in meristem development. 16 The expression analysis of the same gene by genevestigator does not exhibit a result corroborating with the experimental finding.…”

Section: Discussionmentioning

confidence: 99%

Genome wide analysis ofCyclophilingene family from rice and Arabidopsis and its comparison with yeast

Trivedi

Yadav²,

Vaid³

et al. 2012

Plant Signaling & Behavior

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“…Cyclosporin A inhibits both catalytic activities of Cyp proteins: peptidylprolyl cis / transisomerization (PPI) of oligopeptides and the refolding of protein substrates (Fischer et al, 1989). The GNOM-interacting Cyp5 is the product of the Arabidopsis AtCYP5 gene, which recently has been shown to encode a Cyp-like protein with an N-terminal endoplasmic reticulum-transport signal sequence (Saito et al, 1999). Searching for Cyp5-related proteins, we observed closest similarity with putative cytosolic Cyp proteins from nematodes, the plant Digitalis, and Arabidopsis rotamase Cyp protein ROC1, as presented in Figure 6.…”

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confidence: 99%

A Conserved Domain of the Arabidopsis GNOM Protein Mediates Subunit Interaction and Cyclophilin 5 Binding

et al. 2000

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The Arabidopsis GNOM protein, a guanine nucleotide exchange factor (GEF) that acts on ADP ribosylation factor (ARF)-type G proteins, is required for coordination of cell polarity along the apical-basal embryo axis. Interallelic complementation of gnom mutants suggested that dimerization is involved in GNOM function. Here, direct interaction between GNOM molecules is demonstrated in vitro and by using a yeast two-hybrid system. Interaction was confined to an N-terminal domain conserved within a subgroup of large ARF GEFs. The same domain mediated in vitro binding to cyclophilin 5 (Cyp5), which was identified as a GNOM interactor in two-hybrid screening. Cyp5 displayed peptidylprolyl cis / trans -isomerase and protein refolding activities that were sensitive to cyclosporin A. Cyp5 protein accumulated in several plant organs and, like GNOM, was partitioned between cytosolic and membrane fractions. Cyp5 protein was also expressed in the developing embryo. Our results suggest that Cyp5 may regulate the ARF GEF function of the GNOM protein during embryogenesis. INTRODUCTIONThe GNOM gene was identified by multiple mutant alleles in a search for mutations affecting body organization of the Arabidopsis embryo . All gnom alleles are defective in establishing the apical-basal axis of embryo polarity. The earliest defect observed in the gnom embryo, which is a perturbed division of the zygote, is followed by irregular cell division and elongation patterns at subsequent stages (Mayer et al., 1993). gnom seedlings lack a root, are defective in coordinated alignment of vascular cells, and display variably reduced apical structures (Mayer et al., 1993). These alterations have been attributed to defects in the establishment of coordinated cell polarity along the apical-basal axis in early embryos (Steinmann et al., 1999). Cloning of the GNOM gene (also called EMB30 ) revealed sequence similarity to the yeast vesicle trafficking protein Sec7p, including a central region called the Sec7 domain (Shevell et al., 1994;Busch et al., 1996). Proteins with Sec7 domains catalyze guanine nucleotide exchange on small GTP binding proteins of the ADP ribosylation factor (ARF) family required for vesicle coating in membrane trafficking (Chardin et al., 1996;Sata et al., 1998;Springer et al., 1999).Guanine nucleotide exchange factors (GEFs) that act on ARFs (ARF GEFs) group into small and large family members, and large ARF GEFs include the yeast proteins Gea1p, Gea2p, and Sec7p (Chardin et al., 1996;Peyroche et al., 1996;Sata et al., 1998). GNOM is a membrane-associated, functional ARF GEF of the Gea type, suggesting its involvement in vesicular trafficking (Steinmann et al., 1999). Apart from the Sec7 domain, large ARF GEFs contain as yet functionally uncharacterized N-and C-terminal regions . In the case of GNOM, however, there is genetic evidence for subunit interaction, because gnom alleles with different mutations in the Sec7 domain exhibit full complementation (Busch et al., 1996). In this study, we demonstrate a physical interaction of...

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Expression of a Gene for Cyclophilin Which Contains an Amino-Terminal Endoplasmic Reticulum-Targeting Signal

Cited by 42 publications

References 0 publications

Immunophilins and Parvulins. Superfamily of Peptidyl Prolyl Isomerases in Arabidopsis

Immunophilins and Parvulins. Superfamily of Peptidyl Prolyl Isomerases in Arabidopsis

Genome wide analysis ofCyclophilingene family from rice and Arabidopsis and its comparison with yeast

A Conserved Domain of the Arabidopsis GNOM Protein Mediates Subunit Interaction and Cyclophilin 5 Binding

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