The bioinformatics analysis of Prp5 proteins in some model fungi

Abstract:

[Objective] Prp5 proteins were analyzed by bioinformatics in seven model fungi. The purpose is to lay a foundation for further experimental study of Prp5 in RNA splicing and other unique biological function. [Methods] Some basic characteristics, secondary structure, domain and tertiary structure were analyzed and predicted using online webs and softwares in Magnaporthe oryzae, Schizosaccharomyces pombe, Saccharomyces cerevisiae, Neurospora crassa, Aspergillus nidulans, Cryptococcus neoformans and Candida albicans. Meanwhile, the homologies of Prp5 proteins of seven species were compared, based on which a phylogenetic tree was plotted. [Results] The results showed that all studied proteins are unstable hydrophilic protein. Prp5 in Magnaporthe oryzae, Neurospora crassa, Aspergillus nidulans and Prp11 in Schizosaccharomyces pombe were alkaline proteins whereas Prp5 proteins in Cryptococcus neoformans and Candida albicans were acidic. Evolution analysis showed that the seven model fungi are divided into two groups and Magnaporthe oryzae and Neurospora crassa have the closest genetic relationship. Alpha helix is based structure. All proteins contain DEAD and Helicase_C domain. Tertiary structure analysis showed that DEAD domain is stable, while domain Helicase_C showed some changes on the spatial structure. [Conclusion] Prp5 protein may play similar role on account of their conservative structure in different fungi. However, Prp5 protein in Saccharomyces cerevisiae is a little different on spatial structure, suggesting that it may have some unique functions. These results will provide guidance for further study about Prp5 in the experiments.