Systematic Investigation Of Evolutionary Dynamics In Prokaryotes

In this paper,we studied the evolution dynamics of prokaryotes on three levels,gene,operon and protein domain.Take Rhodococcus jostii RHA1 as an example,we discussed the functions of these genes,operons and protein domains which are highly conserved across evolution.As genomics associated with huge data,bioinformatics plays an important role throughout the study.Membrane dynamics are essential for numerous cellular processes in prokaryotic and eukaryotic cells.In eukaryotic cells,membrane fusion and fission are often catalyzed by large GTPases of the Dynamin protein families.While in prokaryotic cells,the study of Dynamin protein families have long been neglected for that most prokaryotes lack of endomembrane systems.During the study of lipid droplet,we found that the lipid droplet exist in PD630 and RHAl.And during the proteomics study of lipid droplet,we found that all of these three Dynamin-like proteins,LPD02062?LPD02063 and ro₀5488 are located on the surface of lipid droplets,and there was a relationship between the size of lipid droplets and the expression quantity of these two proteins,LPD02062 and LPD02063 in PD630.On the basis of such a background,we studied the Dynamin-like protein families.First,we investigated origin and evolution of the Dynamin-like proteins in RHA1.Second,we discussed structure and evolution of the Dynamin-like proteins in RHA1.Third,we concluded localization and partner of the Dynamin-like proteins in bacteria.Fourth,we put forward the hypothesis functional model of the Dynamin-like proteins in RHA1.Through this study that how does the Dynamin-like proteins work in the dynamics of lipid droplet,we expected that we can find a method to improve the formation rate of lipid droplets,and open up a new field for the development of bio-energy.During the process of above research,we found that operons and protein domains are evolutionary dynamics in prokaryotes,but the conservative properties are difference.To explore the dynamic rules of operons and protein domains during the process of evolution,and found the functions of these operons and protein domains which are highly conserved,we did the work as follow.First,we compared the differences of operons between RHA1 and the other 340 prokaryotes.Second,we analyzed the differences of protein domains between RHA1 and the other 340 prokaryotes.Third,we investigated the conservative levels and functions of operons in RHA1.Fourth,we studied the pathways and functions of operons in RHA1.We expected that we can build a whole network to describe the relationship between every two prokaryotes of the 340 prokaryote database.And based on this network,we can study operons and protein domains that we are interested in.All of these are aimed at optimizing pathways artificially.