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Proteins bearing oxidation-induced carbonyl groups are not preferentially ubiquitinated.

Research paper by Marc M Kästle, Tilman T Grune

Indexed on: 16 Mar '11Published on: 16 Mar '11Published in: Biochimie



Abstract

A substantial part of soluble, oxidized proteins are degraded by the proteasome. However, it is still under debate whether these oxidized proteins are degraded by the 26S proteasome in an ubiquitin-dependent way or in an ubiquitin-independent way by the 20S proteasome. Therefore, we treated cells with H(2)O(2) and UV-A irradiation and detected protein carbonyls and ubiquitination by immunoblotting. Separation of ubiquitinated proteins from non-ubiquitinated reveals that most oxidized proteins are not ubiquitinated.