Protein Lysine and Arginine Methylation 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 protein lysine and arginine methylation services in chloroplasts by adding methyl groups to chloroplast proteins (lysine and arginine) to increase the basicity and hydrophobicity of their residues without changing them charge, thereby altering the stability, localization, activity, or protein-protein interactions of the modified protein, precisely to meet customer requirements.

Introduction

Since methylation can occur on nitrogen, carbon and sulfur atoms of protein residues. Therefore, methylation of proteins is a very diverse, extensive and important post-translational modification affecting various aspects of eukaryotic cell biology. In histones and non-histone proteins, methylation occurs mainly on lysine and arginine residues. Methylation of lysines involves the addition of one to three methyl groups to the ε-amine groups of amino acids to form mono-, di-, or tri-methyl lysines. In addition, protein arginine methyltransferases can transfer one or two methyl groups to the terminal nitrogen atom of the guanidine group of an arginine residue. Studies have shown that of the 23 chloroplast methylated proteins identified, 4 contain one or more methylated arginine residues, while 17 proteins have lysine methylation. Identifying non-histone lysine methylation in plants has implications for roles in regulating plant molecular and cellular functions.

Fig. 1. A map of protein lysine methylation in plant cells. (Bienvenut W V, et al., 2020)

Protein Lysine and Arginine Methylation In Chloroplasts Services

With histone modifications, extensive research in the field of epigenetics, and advances in protein mass spectrometry, the understanding of chloroplast protein methylation has grown exponentially. In particular, the chloroplast is one of the best-characterized organelles at the proteomic level. Lifeasible is committed to the proteome-wide identification of chloroplast arginine or lysine methylated proteins and the determination of their methylation sites. In addition, we can assist you in the characterization and functional analysis of identified chloroplast methyl proteins. Our service process is as follows:

• Identification of chloroplast-targeted protein lysine and arginine methyltransferases using bioinformatics methods.
• Mass spectrometry-based method for identification of lysine and arginine methylated proteins in chloroplasts.
• In silico specific identification of high-confidence lysine and arginine methylation sites in chloroplast proteins with different functional classes and subplast positions.
• Perform a visual inspection of the protein's 3D structure and methylation site accessibility.
• A comprehensive analysis of the characteristics and functions of chloroplast methyl proteins.

Applications of Chloroplasts Protein Methylation

• Non-histone lysine methylation in plants regulates protein and protein-nucleic acid interactions, protein stability, subcellular localization, and enzymatic activity, including fundamental cellular processes such as transcription, protein synthesis, signal transduction, and metabolism.
• Chloroplast protein lysine methylation regulates plant molecular and cellular functions.
• Histone methylation, along with acetylation and phosphorylation, can can affect chromatin compaction and up- or down-regulation of gene expression.

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. Serre N B C, Alban C, Bourguignon J, et al. (2018) An outlook on lysine methylation of non-histone proteins in plants[J]. Journal of Experimental Botany. 69(19): 4569-4581.
2. Alban C, Tardif M, Mininno M, et al. (2014) Uncovering the protein lysine and arginine methylation network in Arabidopsis chloroplasts[J]. PLoS One. 9(4): e95512.