Homocysteine thiolactone affects protein ubiquitination in yeast

• Authors: Ewa Bretes , Jarosław Zimny
• Languages of publication: EN

Abstracts

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.

Keywords

EN

homocysteine; homocysteine thiolactone

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2013
• Volume: 60
• Issue: 3
• Pages: 485-488

Dates

published

2013

received

2013-06-13

revised

2013-08-30

accepted

2013-09-09

(unknown)

2013-09-19

Contributors

author

Ewa Bretes

• Poznań University of Life Sciences, Poznań, Poland

author

Jarosław Zimny

• Poznań University of Life Sciences, Poznań, Poland

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