PASTICCINO1 (AtFKBP70) is a nuclear-localised immunophilin required during Arabidopsis thaliana embryogenesis. Carol, R. J., Breiman, A., Erel, N., Vittorioso, P., & Bellini, C. Plant Science, 161(3):527–535, August, 2001. ![PASTICCINO1 (AtFKBP70) is a nuclear-localised immunophilin required during Arabidopsis thaliana embryogenesis [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex The PASTICCINO1 (PAS1) gene of Arabidopsis thaliana encodes a protein with homology to the FK506-binding protein (FKBP) class of immunophilins. To begin to understand more about the possible function of PAS1, we tested some properties of recombinant PAS1 protein and analysed the expression of the gene in Arabidopsis embryos and cell cultures and in tobacco cells. In pas1-1/+ heterozygote embryos the pas1-1 allele is expressed at very low levels in all cells, but it is misexpressed in the pas1-1 homozygote mutant at the same stage. Anti-PAS1 affinity-purified antibodies recognise a 70 kDa protein from dividing cell cultures of Arabidopsis. In indirect immunofluorescence, the same antibodies label the nuclei of dividing tobacco BY-2 cells. In a protease-coupled assay, recombinant PAS1 protein has low peptidylprolyl cis–trans isomerase (PPIase) activity, which is inhibited by the immunosuppressive drugs FK506 and rapamycin, but not by cyclosporin. PAS1 also binds calmodulin in vitro. This data suggests the importance of the correctly regulated production of functional PAS1 protein, a likely nuclear-localised FKBP, for the correct development of the plant embryo.
@article{carol_pasticcino1_2001,
title = {{PASTICCINO1} ({AtFKBP70}) is a nuclear-localised immunophilin required during {Arabidopsis} thaliana embryogenesis},
volume = {161},
issn = {0168-9452},
url = {https://www.sciencedirect.com/science/article/pii/S016894520100437X},
doi = {10/bwth5k},
abstract = {The PASTICCINO1 (PAS1) gene of Arabidopsis thaliana encodes a protein with homology to the FK506-binding protein (FKBP) class of immunophilins. To begin to understand more about the possible function of PAS1, we tested some properties of recombinant PAS1 protein and analysed the expression of the gene in Arabidopsis embryos and cell cultures and in tobacco cells. In pas1-1/+ heterozygote embryos the pas1-1 allele is expressed at very low levels in all cells, but it is misexpressed in the pas1-1 homozygote mutant at the same stage. Anti-PAS1 affinity-purified antibodies recognise a 70 kDa protein from dividing cell cultures of Arabidopsis. In indirect immunofluorescence, the same antibodies label the nuclei of dividing tobacco BY-2 cells. In a protease-coupled assay, recombinant PAS1 protein has low peptidylprolyl cis–trans isomerase (PPIase) activity, which is inhibited by the immunosuppressive drugs FK506 and rapamycin, but not by cyclosporin. PAS1 also binds calmodulin in vitro. This data suggests the importance of the correctly regulated production of functional PAS1 protein, a likely nuclear-localised FKBP, for the correct development of the plant embryo.},
language = {en},
number = {3},
urldate = {2021-11-02},
journal = {Plant Science},
author = {Carol, Rachel J. and Breiman, Adina and Erel, Noa and Vittorioso, Paola and Bellini, Catherine},
month = aug,
year = {2001},
keywords = {Calmodulin, Embryogenesis, FKBP, Nucleus, PPIase},
pages = {527--535},
}
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In pas1-1/+ heterozygote embryos the pas1-1 allele is expressed at very low levels in all cells, but it is misexpressed in the pas1-1 homozygote mutant at the same stage. Anti-PAS1 affinity-purified antibodies recognise a 70 kDa protein from dividing cell cultures of Arabidopsis. In indirect immunofluorescence, the same antibodies label the nuclei of dividing tobacco BY-2 cells. In a protease-coupled assay, recombinant PAS1 protein has low peptidylprolyl cis–trans isomerase (PPIase) activity, which is inhibited by the immunosuppressive drugs FK506 and rapamycin, but not by cyclosporin. PAS1 also binds calmodulin in vitro. 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