Multiubiquitin Chain Binding Subunit MCB1 (RPN10) of the 26S Proteasome Is Essential for Developmental Progression in Physcomitrella patens
| العنوان: | Multiubiquitin Chain Binding Subunit MCB1 (RPN10) of the 26S Proteasome Is Essential for Developmental Progression in Physcomitrella patens |
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| المؤلفون: | Pierre-Alain Girod, Richard D. Vierstra, Hongyong Fu, Jean-Pierre Zryd |
| المصدر: | The Plant Cell. 11:1457-1471 |
| بيانات النشر: | Oxford University Press (OUP), 1999. |
| سنة النشر: | 1999 |
| مصطلحات موضوعية: | Proteasome Endopeptidase Complex, Cytokinins, DNA, Complementary, Saccharomyces cerevisiae Proteins, Protein subunit, Molecular Sequence Data, Plant Science, Physcomitrella patens, Ubiquitin, Amino Acid Sequence, Binding site, Ubiquitins, Gene, Gene Library, Genetics, Indoleacetic Acids, Sequence Homology, Amino Acid, biology, Genetic Complementation Test, Sequence Analysis, DNA, Cell Biology, Plants, Genetically Modified, biology.organism_classification, Bryopsida, Cell biology, Complementation, Proteasome, Mutagenesis, biology.protein, Carrier Proteins, Homologous recombination, Peptide Hydrolases, Protein Binding, Research Article |
| الوصف: | The 26S proteasome, a multisubunit complex, is the primary protease of the ubiquitin-mediated proteolytic system in eukaryotes. We have recently characterized MCB1 (RPN10), a subunit of the 26S complex that has affinity for multiubiquitin chains in vitro and as a result may function as a receptor for ubiquitinated substrates. To define the role of MCB1 further, we analyzed its function in Physcomitrella patens by generating MCB1 gene disruptions using homologous recombination. PpMCB1, which is 50 to 75% similar to orthologs from other eukaryotes, is present in the 26S proteasome complex and has a similar affinity for multiubiquitin chains, using a conserved hydrophobic domain within the C-terminal half of the polypeptide. Unlike yeast Deltamcb1 strains, which grow normally, P. patens Deltamcb1 strains are viable but are under developmental arrest, generating abnormal caulonema that are unable to form buds and gametophores. Treatment with auxin and cytokinin restored bud formation and subsequent partial development of gametophores. Complementation of a Deltamcb1 strain with mutated versions of PpMCB1 revealed that the multiubiquitin chain binding site is not essential for the wild-type phenotype. These results show that MCB1 has an important function in the 26S proteasome of higher order eukaryotes in addition to its ability to bind multiubiquitin chains, and they provide further support for a role of the ubiquitin/26S proteasome proteolytic pathway in plant developmental processes triggered by hormones. |
| تدمد: | 1532-298X 1040-4651 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23ef45f8f4be9284683d002dd11d7fd2Test https://doi.org/10.1105/tpc.11.8.1457Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....23ef45f8f4be9284683d002dd11d7fd2 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 1532298X 10404651 |
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