Homocysteine thiolactone affects protein ubiquitination in yeast

• Autorzy: Bretes E. , Zimny J.
• Języki publikacji: EN

Abstrakty

EN

The formation of homocysteine thiolactone (HcyTl) from homocysteine occurs in all examined so far organisms including bacteria, yeast, and humans. Protein N-homocysteinylation at the ε-amino group of lysine is an adverse result of HcyTl accumulation. Since tagging of proteins by ubiquitination before their proteasomal degradation takes place at the same residue, we wondered how N-homocysteinylation may affect the ubiquitination of proteins. We used different yeast strains carrying mutations in genes involved in the homocysteine metabolism. We found positive correlation between the concentration of endogenous HcyTl and the concentration of ubiquitinated proteins. This suggests that N-homocysteinylation of proteins apparently does not preclude but rather promotes their decomposition.

Słowa kluczowe

EN

homocysteine thiolactone; protein ubiquitination; yeast; homocysteine

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2013
• Tom: 60
• Numer: 3
• Opis fizyczny: p.485-488,fig.,ref.

Twórcy

autor

Bretes E.

• Poznan University of Life Sciences, Poznan, Poland

autor

Zimny J.

• Poznan University of Life Sciences, Poznan, Poland

Bibliografia

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