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Ubiquitin metabolism in Chlamydomonas reinhardtii following cold shock
Author(s) -
Ligr Martin,
Malek Ladislav
Publication year - 1997
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.1399-3054.1997.tb01075.x
Subject(s) - ubiquitin , chlamydomonas reinhardtii , hsp70 , chemistry , protein degradation , metabolism , ubiquitin ligase , chlamydomonas , biochemistry , protein turnover , protein biosynthesis , biophysics , biology , heat shock protein , gene , mutant
The present work characterizes parameters of ubiquitin turnover in Chlamydomonas reinhardtii Dangeard growing under constant temperature conditions and after an exposure to cold shock. The ratio of free and conjugated ubiquitin to total protein and the rate constant of ubiquitin synthesis and conjugation increased about 2‐fold during the first 4 h after cold treatment, whereas the rate constant of ubiquitin degradation reached its maximum 8 h after treatment. The half‐life of ubiquitin calculated from the constant of degradation decreased from 6 h to 3.5 h during the first 4 h after completion of the cold treatment. The rate constant of ubiquitin deconjugation did not change after cold treatment. The ratio of free to conjugated ubiquitin decreased temporarily to approximately 8 immediately after cold treatment and increased back to its original value of about 11 at 2 h after cold treatment. These observations raise questions regarding the regulatory mechanisms of ubiquitin synthesis and degradation.