2013
DOI: 10.18388/abp.2013_2011
|View full text |Cite
|
Sign up to set email alerts
|

Homocysteine thiolactone affects protein ubiquitination in yeast.

Abstract: 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 i… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

0
3
0

Year Published

2020
2020
2023
2023

Publication Types

Select...
3
1

Relationship

0
4

Authors

Journals

citations
Cited by 4 publications
(3 citation statements)
references
References 28 publications
(30 reference statements)
0
3
0
Order By: Relevance
“…1A ). Homocysteine exerts toxic effects through its conversion to S -adenosylhomocysteine, which causes DNA hypomethylation ( 39 , 40 ), or to homocysteine thiolactone, which causes N -homocysteinylation at the ε-amino group of protein lysine residues ( 41 , 42 ). Consequently, we also constructed strains that episomally overexpress genes that could detoxify those products: the S -adenosyl-homocysteinase lyase encoding gene sahL (AFUA_1G10130) or the A. nidulans homocysteine thiolactone hydrolase encoding gene blhA (AN6399) ( A. fumigatus genome does not encode any orthologue) (see Fig.…”
Section: Resultsmentioning
confidence: 99%
“…1A ). Homocysteine exerts toxic effects through its conversion to S -adenosylhomocysteine, which causes DNA hypomethylation ( 39 , 40 ), or to homocysteine thiolactone, which causes N -homocysteinylation at the ε-amino group of protein lysine residues ( 41 , 42 ). Consequently, we also constructed strains that episomally overexpress genes that could detoxify those products: the S -adenosyl-homocysteinase lyase encoding gene sahL (AFUA_1G10130) or the A. nidulans homocysteine thiolactone hydrolase encoding gene blhA (AN6399) ( A. fumigatus genome does not encode any orthologue) (see Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Homycysteinylation is a rare post-translational protein modification. It previously was shown that Hcy-lated proteins were ubiquitinated and degraded via the proteasomal pathway [22].…”
Section: J O U R N a L P R E -P R O O Fmentioning
confidence: 99%
“…1A). Homocysteine exerts toxic effects through its conversion to S-adenosylhomocysteine, which causes DNA hypomethylation (38,39), or to homocysteine thiolactone, which causes N-homocysteinylation at the ε-amino group of protein lysine residues (40,41). Consequently, we also constructed strains that episomally over-express genes that could detoxify those products: the S-adenosyl-homocysteinase lyase encoding gene sahL (AFUA_1G10130) or the A. nidulans homocysteine thiolactone hydrolase encoding gene blhA (AN6399) (A. fumigatus genome does not encode any orthologue) ( Fig.…”
Section: Absence Of Methionine Synthase Enzymatic Activity Results Inmentioning
confidence: 99%