ARC1 is an E3 ubiquitin ligase and promotes the ubiquitination of proteins during the rejection of self-incompatible Brassica pollen
العنوان: | ARC1 is an E3 ubiquitin ligase and promotes the ubiquitination of proteins during the rejection of self-incompatible Brassica pollen |
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المؤلفون: | Sophia L. Stone, Erin M. Anderson, Robert T. Mullen, Daphne R. Goring |
المصدر: | The Plant cell. 15(4) |
سنة النشر: | 2003 |
مصطلحات موضوعية: | Recombinant Fusion Proteins, Ubiquitin-Protein Ligases, Green Fluorescent Proteins, Plant Science, Brassica, Endoplasmic Reticulum, Ligases, Ubiquitin, Tobacco, COP9 signalosome, Ubiquitins, Cells, Cultured, Plant Proteins, biology, Arabidopsis Proteins, COP9 Signalosome Complex, food and beverages, Cell Biology, Subcellular localization, Plants, Genetically Modified, Ubiquitin ligase, Cytosol, Luminescent Proteins, Fertility, Biochemistry, Proteasome, Microscopy, Fluorescence, biology.protein, Pollen, Carrier Proteins, Protein Kinases, Research Article |
الوصف: | ARC1 is a novel U-box protein required in the Brassica pistil for the rejection of self-incompatible pollen; it functions downstream of the S receptor kinase (SRK). Here, we show that ARC1 has E3 ubiquitin ligase activity and contains several motifs that influence its subcellular localization. ARC1 can shuttle between the nucleus, cytosol, and proteasome/COP9 signalosome (CSN) when expressed in tobacco BY-2 suspension-cultured cells. However, ARC1 localization to the proteasome/CSN occurs only in the presence of an active SRK. In the pistil, ubiquitinated protein levels increase specifically with incompatible pollinations, but they do not change in ARC1 antisense-suppressed pistils. In addition, inhibition of the proteasomal proteolytic activity disrupts the self-incompatibility response. We propose that ARC1 promotes the ubiquitination and proteasomal degradation of compatibility factors in the pistil, which in turn leads to pollen rejection. |
تدمد: | 1040-4651 |
الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6853b810b0fab7e51b9efd6f1247396fTest https://pubmed.ncbi.nlm.nih.gov/12671085Test |
حقوق: | OPEN |
رقم الانضمام: | edsair.doi.dedup.....6853b810b0fab7e51b9efd6f1247396f |
قاعدة البيانات: | OpenAIRE |