Protein Acetylation in Chloroplasts

Lifeasible is committed to the development and research of chloroplast engineering. With years of experience in chloroplast proteomics, we are able to provide chloroplast protein acetylation services by N-acetylation of known proteins to change their activity and stability, precisely to meet customer requirements.

Introduction

Acetylation is a type of protein modification controlled by histone acetyltransferases (HATs) and histone deacetylases (HDACs). Acetyl-CoA is a universal metabolite required for many biochemical pathways in plants and a substrate for protein acetylation. Acetylation in plants mainly includes two types: N^α-acetylation and N^ε-acetylation (Lys acetylation). Studies have found that acetylation modification is mainly involved in plant photosynthesis, organ growth and development, stress response and other processes. Among them, irreversible N^α-acetylation of protein N-terminal amino acid residues is one of the most prevalent protein modifications in eukaryotes (including plants) and is involved in many processes in different organisms, such as protein targeting, determination of protein half-life, and mediating of protein-protein interactions. N^ε-acetylation of lysine residues in histones can regulate chromatin remodeling, which in turn controls transcriptional activity. Scientists have identified more than 100 Lys acetylated proteins in plants and more than 20 chloroplast proteins have been identified. Acetylation modifications in plant chloroplasts have become the focus of intensive research.

Fig. 1. A novel protein acetyltransferase family localized or associated to plant plastids is identified and characterised. (Bienvenut W V, et al., 2020)

Protein Acetylation in Chloroplasts Services

Acetylation in chloroplasts is generally much less studied than phosphorylation. However, there are as many as 10 acetylation sites in the α subunit, and the degree of acetylation far exceeds that of phosphorylation. Therefore, acetylation is an important regulator of the photosynthetic chain complex. Lifeasible is committed to the identification of chloroplast protein acetylation sites by performing protein acetylation modification omics analysis in a variety of plants. Our engineers use mass spectrometry, protein structure data, or known structure-function relationships to identify chloroplast acetylated lysines and investigate whether acetylation affects chloroplast protein activity in a variety of ways. Our N^α-acetylation and lysine acetylation services include:

· Identification and Qualitative Assessment of Acetylation
With the help of high-resolution mass spectrometry-based proteomics, we can not only identify specific acetylation sites, but also quantitatively characterize the acetylome.

· Identification and Quantification of Specific Lysines by Mass Spectrometry
We used mass spectrometry to determine the dynamics of relative protein acetylation abundance across various treatments and genetic mutants, and to investigate acetylation site specificity.

· Stoichiometric Assessment of Post-Translationally Modified lysine Site
We provide the stoichiometry or occupancy of acetylated sites by measuring the ratio of endogenous acetylated lysine to unmodified lysine. This is critical for identifying acetylation sites that may have significant effects on protein function.

· Post-Translational Modification Interactions and Crosstalk
We explored the impact on chloroplast protein function by studying the interactions between acetylation and other modifications such as phosphorylation, methylation and ubiquitination.

Applications of Chloroplasts Protein Acetylation

• Some acetylated proteins are involved in photosynthesis and the Calvin cycle and can regulate protein-protein interactions.
• Acetylation modification promotes the expression of chlorophyll synthesis-related genes to enhance plant chlorophyll biosynthesis.
• Lysine acetylated proteins are involved in stimulatory responses, metabolic enzyme activities, cofactor binding, and cellular
• point.
• Regulation of plant responses to pathogens and abscisic acid by histone acetylation on chromatin at target loci.

Lifeasible is committed to developing a variety of cutting-edge technologies to help customers around the world study different types of chloroplast protein modifications. We are proud to regulate plant growth and development, as well as control their pests, through chloroplast protein modifications. If you are interested in our services, please do not hesitate to contact us for more information.

References

1. Schmidt C, Beilsten-Edmands V, Mohammed S, et al. (2017) Acetylation and phosphorylation control both local and global stability of the chloroplast F1 ATP synthase[J]. Scientific reports. 7(1): 1-11.
2. Bienvenut W V, Brünje A, Boyer J B, et al. (2020) Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning protein acetylation[J]. Molecular systems biology. 16(7): e9464.