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Phylogenetic Relationship and Domain Organisation of SET Domain Proteins of Archaeplastida Supriya Sarma* and Mukesh Lodha*

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Phylogenetic Relationship and Domain Organisation of SET Domain Proteins of Archaeplastida Supriya Sarma* and Mukesh Lodha* Sarma and Lodha BMC Plant Biology (2017) 17:238 DOI 10.1186/s12870-017-1177-1 RESEARCHARTICLE Open Access Phylogenetic relationship and domain organisation of SET domain proteins of Archaeplastida Supriya Sarma* and Mukesh Lodha* Abstract Background: SET is a conserved protein domain with methyltransferase activity. Several genome and transcriptome data in plant lineage (Archaeplastida) are available but status of SET domain proteins in most of the plant lineage is not comprehensively analysed. Results: In this study phylogeny and domain organisation of 506 computationally identified SET domain proteins from 16 members of plant lineage (Archaeplastida) are presented. SET domain proteins of rice and Arabidopsis are used as references. This analysis revealed conserved as well as unique features of SET domain proteins in Archaeplastida. SET domain proteins of plant lineage can be categorised into five classes- E(z), Ash, Trx, Su(var) and Orphan. Orphan class of SET proteins contain unique domains predominantly in early Archaeplastida. Contrary to previous study, this study shows first appearance of several domains like SRA on SET domain proteins in chlorophyta instead of bryophyta. Conclusion: The present study is a framework to experimentally characterize SET domain proteins in plant lineage. Keywords: Archaeplastida, Histone modifications, Epigenetics, SET domain, Polycomb, Phylogenetic analysis, Evolution Background deposited by DOT1 methyltransferase that does not Epigenetic cellular memory is heritable during mitosis and/ contain SET domain [13]. meiosis but is not encoded in the genetic material [1, 2]. Based on SET domain sequence similarity to Drosoph- Histone post-translational modifications, DNA methyla- ila homologues, plant SET domain proteins are classified tion, and non-coding RNAs and chromatin remodelling into 4 main classes [14], Enhancer of Zeste, E(z) homo- are the major components of epigenetic inheritance [3]. logs; Absent, Small, or Homeotic disks (Ash) homologs Numerous histone modifications like acetylation, methyla- and related proteins; Trithorax (Trx) homologs and re- tion and phosphorylation occur mainly in the N-terminal lated proteins; and Suppressor of Variegation, Su(var) tails of the histones [2, 4–6]. These histone modifications homologs and related proteins [14–16]. Su(var) and E(z) are associated with transcriptional repression or activation, group proteins are mainly involved in transcription re- DNA repair and DNA recombination [7]. Among various pression, whereas Trx and Ash group are mainly in- histone modifications, lysine methylation is rigorously volved in transcriptional de-repression [16, 17]. A studied in plant, fungi, and animal models [8, 9]. Lysine separate category is later added to include proteins with residues can be mono, di and tri-methylated [8]. Lysine an interrupted SET domain, lowly conserved SET methylation is catalyzed by 130–150 amino acid domain and proteins with TPR and Rubisco domains protein domain. The name SET is derived from Dros- [18–20]. This category of proteins are not well charac- ophila proteins, Su(var)3–9 [10], Enhancer of zeste, terized for their biochemical activity. E(z) [11], and Trithorax (trx)[12]havingthisdomain. Here we have taken a computational approach to ana- The only exception is the H3K79 methylation mark lyse SET domain sequences of 16 different taxa of Archaeplastida. 506 SET proteins are identified that are classified into five classes. Our work will serve as a * Correspondence: [email protected]; [email protected] Centre for Cellular and Molecular Biology (CSIR), Uppal Road, Habsiguda, guideline for functional and biochemical characterization Hyderabad 500007, India of SET proteins of plant lineage. © The Author(s). 2017 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. Sarma and Lodha BMC Plant Biology (2017) 17:238 Page 2 of 12 Methods SET domain and their associated domain using NCBI Identification of SET domain proteins in Archaeplastida Batch CD search tool (http://www.ncbi.nlm.nih.gov/Struc- To uncover the SET proteins in Archaeplastida, the con- ture/bwrpsb/bwrpsb.cgi/) and NCBI-CD Hit (https://ww served SET domain amino acid sequences from Arabidop- w.ncbi.nlm.nih.gov/Structure/cdd/wrpsb.cgi). sis thaliana (At), Oryza sativa (Os), Picea abies (Pa), Selaginella meollendorffii (Sm), Physcomitrella patens (Pp), Phylogenetic analysis Micromonas pusila (Mpu), Micromonas RCC299 (Mr), For phylogenetic tree construction, 251 SET domain se- Ostreococcus tauri (Ot), Ostreococcus lucimerinus (Ol), quences retrieved from the E(z), Ash, Trx and Su(var) Chlorella vulgaris (Cv), Chlamydomonas reinhardtii (Cr) group are included. SET domain containing proteins from and Volvox carteri (Vc) are retrieved by BLAST search the Orphan, SETD, and TPR are excluded due to low se- using SET domain (PF00856) as query from PFAM data- quence similarity with E(z), Ash, Trx and Su(var). Multiple base Version 30.0 (http://pfam.xfam.org/family/PF00856) sequence alignments of SET domain sequences are per- [21]. The SET domain protein sequences are also retrieved formed using the ClustalW program. Evolutionary ana- from Uniprot (http://www.uniprot.org/) and Phytozome lyses are conducted in MEGA7.0 program [22]. The v12.1 (https://phytozome.jgi.doe.gov/pz/portal.html) that evolutionary history is inferred by using the Maximum are not available in PFAM. To better understand the Likelihood method based on the JTT matrix based model evolutionary history and functionality of SET domain- with a bootstrap test of 1000 replicates for internal branch containing proteins in plant lineages, we have use reliability and use all sites option as Gaps/Missing data assembled transcriptome data from, Nitella mirabilis treatment. The tree with the highest log likelihood (Nm) (https://www.ncbi.nlm.nih.gov/bioproject/ (−39,059.190) is shown. Initial tree(s) for the heuristic PRJNA158153 158153), Klebsormidium flaccidum (Kf) search are obtained automatically by applying Neighbour- (https://www.ncbi.nlm.nih.gov/bioproject/ PRJNA 51159). Joining and BioNJ algorithms to a matrix of pairwise dis- Cyanophora paradoxa (http://cyanophora.rutgers.edu/ tances estimated using a JTT model, and then selecting cyanophora/) and predicted proteome data for Marchantia the topology with superior log likelihood value. polymorpha (Mp) (https://www.ncbi.nlm.nih.gov/biopro- ject/PRJNA218052) and Gymnosperm, Picea abies (Pa) Multiple alignments of SET domain sequences (http://marchantia.info/tom/blast/blast.html tom/blast/ Multiple sequence alignment is performed for the unan- blast.html). In in silico proteome datasets, if two or more notated conserved SET domain sequences of plant line- overlapping protein sequences arose from same genetic ages with reference Arabidopsis and rice SET domain locus, we have selected the longest sequence. Transcript sequences using multalin program (http://multalin.tou- sequences obtained from NCBI website are transdecoded louse.inra.fr/multalin/) with the default parameters. SET into predicted proteins using Transdecoder ( https://trans- domain sequences sharing significant homology with decoder.github.io/) that gave the longest open reading Arabidopsis and rice. SET domain sequences are catego- frame. Local Blastp (ftp://ftp.ncbi.nlm.nih.gov/blast/exe- rized to the corresponding group of the SET domain. cutables/blast+/LATEST/. nih.gov/blast/executables/blast Classification is also interpreted based on neighbouring +/LATEST/) is carried out with these predicted proteins domain organization. against 130–150 length SET domain sequences from Arabi- dopsis thaliana to filter the SET domain containing sequences. Thereafter, redundant SET domain amino acid Nomenclature and classification of SET domain proteins sequences are removed from all the SET domain sequences SET domain proteins are named according to the obtained from the online search. The Arabidopsis thaliana nomenclature of annotated plant and animal SET do- and Oryza sativa SET domains protein sequences are used main histone methyltransferases with generic capital- as queries because it is a representative of flowering plants ized letter followed by species name in the lower case and possess relatively complete annotated protein using the common specific protein name. SET do- information. main proteins are named according to the name of the closest Arabidopsis thaliana and Oryza sativa Domain architecture homolog. If two or more proteins were equally close Presence or absence of specific domain and its organ- to a single Arabidopsis thaliana and Oryza sativa isation might provide an intimation to the functional SET domain containing proteins, then the same name divergence of the different protein groups. Addition- is used followed by the letters “a”, “b”,etc.Thefol- ally, it is conventional that proteins sharing identical lowing nomenclature is adopted for classes and sub- domain may share close evolutionary relationship and classes of the SET domain-containing proteins: For
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