Analysis of Chloroplast Outer and Inner Membrane Proteins

The chloroplast is surrounded by a double membrane system, an inner and outer membrane, and separates the chloroplast stroma from the cytoplasm. Studies have found that the inner and outer membranes of chloroplasts are very different in composition and function. The outer membrane contains membrane pores that allow the passage of substances with a molecular weight of less than 10 kD. However, a large number of enzymes related to photosynthesis are attached to the inner membrane of the inner membrane, which has a strong selectivity for the permeability of substances. In addition, some specific transport proteins and ion channels in the inner membrane of chloroplasts play an important role in controlling and coordinating interstitial and cytoplasmic metabolism. The scientists developed a targeted hydrophobic and subcellular-specific proteomic approach to identify components of the hydrophobic core of the chloroplast envelope. Many key molecules in the cytoplasm, receptors on the surface of organelles, and intercalases that facilitate insertion into the outer membrane of the chloroplast remain unknown. Therefore, studying the chloroplast inner and outer membrane proteome is crucial for understanding chloroplast biological pathways and their regulation.

Fig. 1. Sample preparation for proteome studies and annotation of envelope proteins by proteome data and molecular features. (Trentmann O, et al., 2020)

Services

In recent years, with the development of proteomics and the development of more powerful bioinformatics tools, an increasing number of chloroplast inner and outer membrane proteins have been identified and characterized. However, the specific mechanisms of many outer membrane proteins remain undetermined. Over the years, the team at Lifeasible has extensive experience in chloroplast membrane protein analysis. We are committed to using proteomic in silico approaches to discover novel envelope transporters, as well as to identify known and newly discovered putative envelope proteins Common features of membrane transporters. In addition, we used a proteome-wide bioinformatics approach to identify novel chloroplast outer membrane protein targeting signals and pathways. Our chloroplast inner and outer membrane protein analysis service process is as follows:

(1) Purification of the chloroplast envelope.
(2) Isolation of chloroplast envelope proteins.
(3) Identification of chloroplast envelope proteins by mass spectrometry.
(4) Identification of chloroplast envelope transport systems with common features.
(5) Providing biological information for database mining based on proteomics.

Competitive Advantages

• Highly purified chloroplast envelope proteome, distinguishing true envelope proteins from contaminants.
• Advanced SDS/PAGE separation and tandem mass spectrometry.
• Envelope localization combined with MS-based spectral count analysis and manual annotation.
• Building a virtual database of chloroplast envelope proteins.
• Discovery of previously unknown components of the chloroplast envelope.

Lifeasible can meet the needs of customers on time and on budget through a wide range of strategies for analyzing chloroplast proteome. Our aim is to be customer-centric and to provide the highest quality service to customers around the world. Our skilled and dedicated scientific researchers ensure that the most appropriate methods and techniques are selected for each specialized chloroplast project. Our customer service representatives are enthusiastic and trustworthy 24 hours a day, 7 days a week. If you are interested in our services, please feel free to contact us  for more information or a detailed discussion.

References

1. Trentmann O, Mühlhaus T, Zimmer D, et al. (2020) Identification of chloroplast envelope proteins with critical importance for cold acclimation[J]. Plant Physiology. 182(3): 1239-1255.
2. Ferro M, Salvi D, Rivière-Rolland H, et al. (2002) Integral membrane proteins of the chloroplast envelope: identification and subcellular localization of new transporters[J]. Proceedings of the National Academy of Sciences. 99(17): 11487-11492.