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The ubiquitin system in plants
Author(s) -
Kampen Jan,
Wettern Michael,
Schulz Margot
Publication year - 1996
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1996.tb00523.x
Subject(s) - ubiquitin , proteasome , microbiology and biotechnology , ubiquitin ligase , transcription factor , biology , protein degradation , ubiquitins , yeast , biochemistry , chemistry , gene
The small polypeptide ubiquitin participates in a variety of fundamental cellular events, such as cell differentiation, stress response, determination of steady state levels of regulatory proteins, cell cycle control, regulation of transcription, and programmed cell death. Although the complex mechanisms of these processes are not fully understood, ubiquitinylation of regulatory proteins involved in those events is obviously essential. Target proteins can be covalently coupled with one or a few ubiquitin molecules, which is supposed to present a (reversible) post‐translational modification. Polyubiquitinylation, however, marks proteins selectively for degradation by the 26S proteasome. The ubiquitin system has been studied mostly with animal systems or yeast, but all basic reactions of ubiquitin appear in plants as well. The scope of this review is to summarize several implications of recent studies directed towards the plant ubiquitin system.