{"title":"In silico analysis of dicer-like protein (DCLs) sequences from higher plant species","authors":"E. Filiz, I. Koc","doi":"10.18478/IUFSJB.31589","DOIUrl":null,"url":null,"abstract":"Dicer and Dicer like (DCLs) proteins are essential part of small RNA biogenesis pathway, is a type of RNase III digesting long dsRNA (pre-miRNA) to small RNA segments (miRNA). A total of 20 full length of Dicer like proteins (DCL1, DCL2, DCL3 and DCL4) from different organisms available in NCBI were evaluated by bioinformatics tools to investigate properties, structure of DCLs, domain analysis, multiple sequence alignment and phylogenetics tree construction. All DCLs protein sequences have Ribonuclease III protein family that contains RNaseIII domain including Helicase ATP-binding type-1, Helicase C-terminal, Dicer double-stranded RNA-binding fold, PAZ, Ribonuclease III, Double stranded RNA-binding domain (dsRB). Physicochemical analysis offers data such as pI, EC, Al, GRAVY and instability index about these enzymes. Putative phosphorylation sites were also identified which are found to be conserved in plant species and the results showed that the most abundant phosphorylation site is Serine residues in DCLs proteins. Patterns and profile analysis were performed using Prosite and conserved protein motifs subjected to MEME to obtain the best possible matches. The phylogenetics tree represented three major clusters and similar DCLs protein sequences of different plant species clustered together. The obtained results could be used for further in silico analysis and homology modeling studies. Keywords: Dicer, DCLs, miRNA, RNase, In silico analysis. *Corresponding Author: Ertugrul Filiz (e-mail: ertugrulfiliz@gmail.com). (Received: 25.05.2012 Accepted: 24.01.2013)","PeriodicalId":14521,"journal":{"name":"IUFS Journal of Biology","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2013-11-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"4","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"IUFS Journal of Biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.18478/IUFSJB.31589","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 4
Abstract
Dicer and Dicer like (DCLs) proteins are essential part of small RNA biogenesis pathway, is a type of RNase III digesting long dsRNA (pre-miRNA) to small RNA segments (miRNA). A total of 20 full length of Dicer like proteins (DCL1, DCL2, DCL3 and DCL4) from different organisms available in NCBI were evaluated by bioinformatics tools to investigate properties, structure of DCLs, domain analysis, multiple sequence alignment and phylogenetics tree construction. All DCLs protein sequences have Ribonuclease III protein family that contains RNaseIII domain including Helicase ATP-binding type-1, Helicase C-terminal, Dicer double-stranded RNA-binding fold, PAZ, Ribonuclease III, Double stranded RNA-binding domain (dsRB). Physicochemical analysis offers data such as pI, EC, Al, GRAVY and instability index about these enzymes. Putative phosphorylation sites were also identified which are found to be conserved in plant species and the results showed that the most abundant phosphorylation site is Serine residues in DCLs proteins. Patterns and profile analysis were performed using Prosite and conserved protein motifs subjected to MEME to obtain the best possible matches. The phylogenetics tree represented three major clusters and similar DCLs protein sequences of different plant species clustered together. The obtained results could be used for further in silico analysis and homology modeling studies. Keywords: Dicer, DCLs, miRNA, RNase, In silico analysis. *Corresponding Author: Ertugrul Filiz (e-mail: ertugrulfiliz@gmail.com). (Received: 25.05.2012 Accepted: 24.01.2013)