Relationship between RGS protein types and physicochemical properties in fungi

Abstract:

[Objective] As a negative regulator of G protein signal transduction pathway, G protein signal regulator factor plays an important role in the pathogenicity asexual reproduction regulation of plant pathogens. To identify the relationship between RGS protein types and their physicochemical properties in fungi. [Methods] We analyzed 229 of previously identified RGS protein sequences in 49 fungi including model organism, pathogenic bacteria and non-pathogenic bacteria, and identified 6 proteins according to their conserved domains, such as DEP-RGS, RGS-TM, PXA-RGS-PX, RGS, RGS-PAS-PAC and TM-RGS. We used the protein database, ProtComp v9.0, PHD and MEME to analyze the physicochemical properties, subcellular localization, secondary structure and motif of the above RGS proteins. [Results] The above-mentioned different types of RGS proteins had obvious characteristic futures, and following common characteristics: theoretical isoelectric point was between 6.01 and 7.00, instability coefficients were between 40.01 and 60.00, more than 95% of RGS proteins were hydrophilic protein, the strongest hydrophilic amino acid residues were arginine, aspartic acid, glutamic acid, glutamine, asparagine, the strongest hydrophobic amino acid residues were leucine, alanine, valine, phenylalanine, isoleucine, the secondary structure was characterized by less Beta strand, situation for the transit peptide situation is unclear, and subcellular location is more concentrated in the nucleus. [Conclusion] The physicochemical properties of the six RGS proteins have some common characteristics, but different types of RGS proteins also have obvious category characteristics, mainly in the conserved domain, secondary structure, isoelectric point, transport peptide and subcellular localization.