Chloroplast Engineering - Lifeasible
Protein Glycosylation in Chloroplasts
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Protein Glycosylation in Chloroplasts

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Lifeasible is committed to the development and research of chloroplast engineering. With years of experience in chloroplast proteomics, we are able to provide protein glycosylation services in the chloroplast, by glycosylating related enzymes to change their catalytic activity, thermostability, folding and subcellular localization, and plant immunity, precisely to meet customer requirements.


Introduction

Protein glycosylation is the addition of carbohydrates to proteins, including N-linked glycosylation, O-linked glycosylation, Glycosylphosphatidylinositol (GPI), proteoglycans, and O-linked N-acetylglucosamine (O-GlcNAc) etc. Among them, N-glycosylation is the most common protein post-translational modification in plants and is the key to protein entry into the secretory pathway. Studies have shown that glycosylation modification is involved in various biological processes such as signal transmission, photosynthesis, flowering regulation, cell wall synthesis, and disease resistance in plants. It was initially thought that there were no glycoproteins in the chloroplast proteome, because the transfer of bulky proteins across the double-membrane envelope via transposons of the chloroplast envelope was thought to be impossible. However, scientists have successfully identified some chloroplast glycoproteins and found 2186 N-glycosylation sites in Arabidopsis.

Schematic overview of complexN-glycan processing in plants.Fig. 1. Schematic overview of complexN-glycan processing in plants. (Schoberer J, et al., 2018)

Protein Glycosylation in Chloroplasts Services

Studies have found that N-glycosylation plays a key role in regulating plant stress resistance and maintaining photosynthetic efficiency. In addition, defects in the glycosylation machinery will have implications for plant development and growth. Lifeasible is committed to identifying glycosylated proteins and glycosylation sites in chloroplasts of a variety of plants. Additionally, we can help you analyze the impact of N-glycosylation on the functional role of these proteins. Our chloroplast protein glycosylation services include:

· N-Linked Glycosylation
N-glycosylation is shown to occur in the endoplasmic reticulum and the Golgi apparatus, and is then transported to the chloroplast via the vesicular Golgi-to-plastid transport pathway. Our engineers can identify glycosylated proteins in the chloroplast matrix by a variety of methods and predict glycosylation sites in silico.

· O-Linked Glycosylation
O-glycosylated proteins are involved in cell wall formation and plant immunity. Our engineers can identify O-glycosylation sites in Arabidopsis and explore how glycosylation regulates plant development through epigenetic modifications.

Applications of Chloroplasts Protein Glycosylation

  • The glycosylation status of some proteins can serve as a signal of the overall energy state of the cell.
  • N-glycosylation of proteins involved in photosynthesis and carbon metabolism to regulate carbohydrate metabolism and plant developmental processes.
  • Different types of target proteins, such as those related to cell wall synthesis, metabolism, redox, and proteolysis, are modified by glycosylation, thereby coordinating the biological development process of plants.
  • Evasion of host immune responses by N-glycosylation of phytopathogenic effector proteins.

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. Jiao Q S, Niu G T, Wang F F, et al. (2020) N-glycosylation regulates photosynthetic efficiency of Arabidopsis thaliana[J]. Photosynthetica. 58(1): 72-79.
  2. Schoberer J, Strasser R. (2018) Plant glyco-biotechnology[C]//Seminars in Cell & Developmental Biology. Academic Press. 80: 133-141.
For research use only, not intended for any clinical use.
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