Emerging functions for nonhistone protein acetylation in budding yeast.

Area of Science:

• Biochemistry
• Molecular Biology
• Cell Biology

Background:

• Lysine acetylation is a key post-translational modification (PTM).
• Traditionally studied on histones, nonhistone protein acetylation is now recognized as widespread in eukaryotes.
• Advances in mass spectrometry (MS) reveal widespread protein acetylation, yet functional studies lag behind.

Purpose of the Study:

• To review the functional roles of lysine acetylation on nonhistone proteins.
• To highlight acetylation's involvement in chromatin remodeling, DNA repair, protein homeostasis, and cell cycle metabolic coordination.
• To discuss emerging themes and open questions in nonhistone protein acetylation research.

Main Methods:

• Literature review of studies on Saccharomyces cerevisiae.
• Analysis of mass spectrometry data identifying acetylated proteins.
• Functional analysis of specific nonhistone protein acetylation sites.

Main Results:

• Acetylation regulates diverse cellular pathways, including chromatin remodeling and DNA damage repair.
• Nonhistone protein acetylation plays critical roles in maintaining protein homeostasis.
• Acetylation is involved in the metabolic coordination of the cell cycle.

Conclusions:

• Lysine acetylation is a crucial regulatory mechanism for nonhistone proteins.
• Further research is needed to elucidate the functional significance of many identified acetylations.
• Understanding nonhistone acetylation offers insights into fundamental cellular processes and potential therapeutic targets.