BARROS, B. A.

DAMASCENO, C. M. B.

MACIEL, L. S.

MAGALHAES, J. V.

SOUSA, S. M. de

English

Repository Open Access to Scientific Information from Embrapa

     PHYLOGENETIC ANALYSIS AND FUNCTIONAL CHARACTERIZATION OF SbPSTOL1 PROTEINS IN SORGHUM         Maciel, L.S.1,2; Barros, B.A.1; Damasceno, C.M.B.1; De Sousa, S.M.1; Magalhães, J.V.1,2   1Embrapa Milho e Sorgo, Rod. MG 424, Km 45 - Sete Lagoas, MG  2Departamento de Biologia Geral do Instituto de Ciências Biológicas, UFMG     laianesm@gmail.com   Palavra-chave: Phylogeny RLKs, stress abiotic, stress biotic, Poaceae, cis regulatory elements     Receptor-like kinases (RLKs)/Pelle belong to a monophyletic group of the serine/threonine protein kinase superfamily. These proteins play key roles during cellular development and activate signaling pathways in response to environmental stimuli. Phosphorus starvation tolerance 1 (PSTOL1) genes in rice (OsPSTOL1) and sorghum (SbPSTOL1) are similar to members of the superfamily RLKs/Pelle and are linked to root morphology and phosphorus (P) acquisition. Here, we report on a phylogenetic analysis, an in silico analysis of cis regulatory elements and subcellular localization of these proteins. We also studied the expression profiling of SbPSTOL1 in response to P using sorghum lines contrasting for root morphology traits. Kinase domain alignment of different members of the superfamily RLKs/Pelle was performed with ClustalW and a phylogenetic tree was constructed using the maximum likelihood method (JTT model, with 1000 bootstrap replicates) implemented in the MEGA7 software. Predictions of the protein domains were carried out using Pfam and Smart tools. Analyses of the upstream region, approximately 2000 bp, of each gene (OsPSTOL1 and SbPSTOL1) were performed using the MatInspector software. Transient expression 35S::SbPSTOL1::GFP was achieved via particle bombardment of onion epidermal cells. The kinase domain (predicted to be cytoplasmic) is conserved among 6 selected SbPSTOL1 proteins but the N-terminus differs, featuring a putative extracellular domain containing a signal peptide, a cysteine-rich galacturonan_binding domain (GUB-WAK_bind), a wall-associated receptor kinase domain (WAK_assoc domain) and a transmembrane domain. Phylogenetic and structural analysis support that OsPSTOL1 in rice and SbPSTOL1 in sorghum are both members of the LRK10 subfamily and share a common ancestry. SbPSTOL1 proteins were highly similar to ZmWAKRLK in maize, which confers resistance to Exserohilum turcicum and represents a new class of immunological receptors in monocots. In silico analysis of cis regulatory elements suggest that OsPSTOL1 and SbPSTOL1 genes can respond to environmental stimuli such as biotic and abiotic stresses. In fact, SbPSTOL1 was transcriptionally upregulated by low P and showed a tendency towards increased expression in lines that have higher root surface area. The subcellular localization of the OsPSTOL1 protein is predicted to be cytoplasmic. However, the possible presence of cell-wall association domains as well transmembrane domains in SbPSTOL1 proteins warrants our current efforts to confirm SbPSTOL1 as functional wall-associated kinases (WAKs). We hypothesize that SbPSTOL1 proteins, which are members of the subfamily LRK10, have the capacity to monitoring the extracellular environment, thereby inducing signaling pathways involved in adaptive responses to abiotic and biotic stress.   Supported by CNPq, Fapemig and Embrapa Resumos do VI SBGMP • 28 de maio a 2 de junho de 2017 Parque Metalúrgico Augusto Barbosa Centro de Artes e Convenções da UFOP • Ouro Preto • MG  www.sbg.org.br - ISBN978-85-89109-06-2 VI Simpósio Brasileiro de Genética Molecular de Plantas 

Phylogenetic analysis and functional characterization of SbPSTOL1 proteins in sorghum.

http://www.alice.cnptia.embrapa.br/bitstream/doc/1076600/1/Phylogeneticanalysis.pdf

Phylogenetic analysis and functional characterization of SbPSTOL1 proteins in sorghum.

Abstract

Similar works

Full text

Available Versions

Repository Open Access to Scientific Information from Embrapa