Control of protein function by reversible Nɛ-lysine acetylation in bacteria
✍ Scribed by Sandy Thao; Jorge C Escalante-Semerena
- Book ID
- 116747773
- Publisher
- Elsevier Science
- Year
- 2011
- Tongue
- English
- Weight
- 303 KB
- Volume
- 14
- Category
- Article
- ISSN
- 1369-5274
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It is now becoming apparent that cross-talk between two protein lysine modifications, acetylation and ubiquitination, is a critical regulatory mechanism controlling vital cellular functions. The most apparent effect is the inhibition of proteasome-mediated protein degradation by lysine acetylation.
Young developing seedlings of Mimulus cardinalis Douglas (Scrophulariaceae) were grown in Hoagland's medium supplemented with lysine (LYS; 1.0 mM), threonine (THR; 1.0 mM),LYSq-THR (1.0 mMea.) or Lu (MET; 1.0 1.0-0.1raM, respectively). LYS or THR reduced the total amount of protein in the developing