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Active oxygen induced protein ubiquitination in Chlamydomonas
Author(s) -
Shimogawara Kousuke,
Muto Shoshi
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80130-u
Subject(s) - chlamydomonas , hydrogen peroxide , ubiquitin , oxygen , chemistry , superoxide , reactive oxygen species , active oxygen , biochemistry , biophysics , microbiology and biotechnology , photochemistry , biology , enzyme , mutant , gene , organic chemistry
When methylviologen‐treated Chlamydomonas cells were exposed to light, the amount of ubiquitinated proteins with molecular masses of 28‐ and 31‐kDa were drastically changed, i.e. the former increased within 20 min illumination, while the latter decreased. Since these changes are completely dependent on illumination and suppressed by adding 3‐(3,4‐dichlorophenyl)‐1, 1‐dimethylurea, it was concluded that these changes were caused by active oxygen stress. Treating cells with hydrogen peroxide did not cause such changes of ubiquitination, suggesting that the molecular species of active oxygen is a superoxide anion.