RESUMEN
Human aromatase enzyme is a microsomal cytochrome P450 and catalyzes aromatization of androgens into estrogens during steroidogenesis. For breast cancer therapy, third-generation aromatase inhibitors (AIs) have proven to be effective; however patients acquire resistance to current AIs. Thus there is a need to predict aromatase-related proteins to develop efficacious AIs. A machine learning method was established to identify aromatase-related proteins using a five-fold cross validation technique. In this study, different SVM approach-based models were built using the following approaches like amino acid, dipeptide composition, hybrid and evolutionary profiles in the form of position-specific scoring matrix (PSSM); with maximum accuracy of 87.42%, 84.05%, 85.12%, and 92.02% respectively. Based on the primary sequence, the developed method is highly accurate to predict the aromatase-related proteins. Prediction scores graphs were developed using the known dataset to check the performance of the method. Based on the approach described above, a webserver for predicting aromatase-related proteins from primary sequence data was developed and implemented at https://bioinfo.imtech.res.in/servers/muthu/aromatase/home.html. We hope that the developed method will be useful for aromatase protein related research.
Asunto(s)
Aromatasa , Proteínas , Humanos , Aromatasa/genética , Proteínas/química , Aminoácidos/química , Evolución Biológica , Aprendizaje AutomáticoRESUMEN
BACKGROUND: Rhodopsin is a seven-transmembrane protein covalently linked with retinal chromophore that absorbs photons for energy conversion and intracellular signaling in eukaryotes, bacteria, and archaea. Haloarchaeal rhodopsins are Type-I microbial rhodopsin that elicits various light-driven functions like proton pumping, chloride pumping and Phototaxis behaviour. The industrial application of Ion-pumping Haloarchaeal rhodopsins is limited by the lack of full-length rhodopsin sequence-based classifications, which play an important role in Ion-pumping activity. The well-studied Haloarchaeal rhodopsin is a proton-pumping bacteriorhodopsin that shows promising applications in optogenetics, biosensitized solar cells, security ink, data storage, artificial retinal implant and biohydrogen generation. As a result, a low-cost computational approach is required to identify Ion-pumping Haloarchaeal rhodopsin sequences and its subtype. RESULTS: This study uses a support vector machine (SVM) technique to identify these ion-pumping Haloarchaeal rhodopsin proteins. The haloarchaeal ion pumping rhodopsins viz., bacteriorhodopsin, halorhodopsin, xanthorhodopsin, sensoryrhodopsin and marine prokaryotic Ion-pumping rhodopsins like actinorhodopsin, proteorhodopsin have been utilized to develop the methods that accurately identified the ion pumping haloarchaeal and other type I microbial rhodopsins. We achieved overall maximum accuracy of 97.78%, 97.84% and 97.60%, respectively, for amino acid composition, dipeptide composition and hybrid approach on tenfold cross validation using SVM. Predictive models for each class of rhodopsin performed equally well on an independent data set. In addition to this, similar results were achieved using another machine learning technique namely random forest. Simultaneously predictive models performed equally well during five-fold cross validation. Apart from this study, we also tested the own, blank, BLAST dataset and annotated whole-genome rhodopsin sequences of PWS haloarchaeal isolates in the developed methods. The developed web server ( https://bioinfo.imtech.res.in/servers/rhodopred ) can identify the Ion Pumping Haloarchaeal rhodopsin proteins and their subtypes. We expect this web tool would be useful for rhodopsin researchers. CONCLUSION: The overall performance of the developed method results show that it accurately identifies the Ionpumping Haloarchaeal rhodopsin and their subtypes using known and unknown microbial rhodopsin sequences. We expect that this study would be useful for optogenetics, molecular biologists and rhodopsin researchers.