Your browser doesn't support javascript.
loading
Identification and characterization of aquaporin genes in Arachis duranensis and Arachis ipaensis genomes, the diploid progenitors of peanut.
Shivaraj, S M; Deshmukh, Rupesh; Sonah, Humira; Bélanger, Richard R.
Affiliation
  • Shivaraj SM; Département de phytologie-Faculté des Sciences de l'agriculture et de l'alimentation, Université Laval, 2425 rue de l'Agriculture, Québec City, QC, G1V 0A6, Canada.
  • Deshmukh R; National Agri-Food Biotechnology Institute (NABI), Mohali, India.
  • Sonah H; National Agri-Food Biotechnology Institute (NABI), Mohali, India.
  • Bélanger RR; Département de phytologie-Faculté des Sciences de l'agriculture et de l'alimentation, Université Laval, 2425 rue de l'Agriculture, Québec City, QC, G1V 0A6, Canada. richard.belanger@fsaa.ulaval.ca.
BMC Genomics ; 20(1): 222, 2019 Mar 18.
Article in En | MEDLINE | ID: mdl-30885116
BACKGROUND: Aquaporins (AQPs) facilitate transport of water and small solutes across cell membranes and play an important role in different physiological processes in plants. Despite their importance, limited data is available about AQP distribution and function in the economically important oilseed crop peanut, Arachis hypogea (AABB). The present study reports the identification and structural and expression analysis of the AQPs found in the diploid progenitor genomes of A. hypogea i.e. Arachis duranensis (AA) and Arachis ipaensis (BB). RESULTS: Genome-wide analysis revealed the presence of 32 and 36 AQPs in A. duranensis and A. ipaensis, respectively. Phylogenetic analysis showed similar numbers of AQPs clustered in five distinct subfamilies including the plasma membrane intrinsic proteins (PIPs), the tonoplast intrinsic proteins (TIPs), the nodulin 26-like intrinsic proteins (NIPs), the small basic intrinsic proteins (SIPs), and the uncharacterized intrinsic proteins (XIPs). A notable exception was the XIP subfamily where XIP1 group was observed only in A. ipaensis genome. Protein structure evaluation showed a hydrophilic aromatic/arginine (ar/R) selectivity filter (SF) in PIPs whereas other subfamilies mostly contained a hydrophobic ar/R SF. Both genomes contained one NIP2 with a GSGR SF indicating a conserved ability within the genus to uptake silicon. Analysis of RNA-seq data from A. hypogea revealed a similar expression pattern for the different AQP paralogs of AA and BB genomes. The TIP3s showed seed-specific expression while the NIP1s' expression was confined to roots and root nodules. CONCLUSIONS: The identification and the phylogenetic analysis of AQPs in both Arachis species revealed the presence of all five sub-families of AQPs. Within the NIP subfamily, the presence of a NIP2 in both genomes supports a conserved ability to absorb Si within plants of the genus. The global expression profile of AQPs in A. hypogea revealed a similar pattern of AQP expression regardless of the subfamilies or the genomes. The tissue-specific expression of AQPs suggests an important role in the development and function of the respective organs. The AQPs identified in the present study will serve as a resource for further characterization and possible exploitation of AQPs to understand their physiological role in A. hypogea.
Subject(s)
Key words

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Arachis / Plant Proteins / Genome, Plant / Gene Expression Regulation, Plant / Aquaporins Type of study: Diagnostic_studies Language: En Journal: BMC Genomics Journal subject: GENETICA Year: 2019 Document type: Article Affiliation country: Canada Country of publication: United kingdom

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Arachis / Plant Proteins / Genome, Plant / Gene Expression Regulation, Plant / Aquaporins Type of study: Diagnostic_studies Language: En Journal: BMC Genomics Journal subject: GENETICA Year: 2019 Document type: Article Affiliation country: Canada Country of publication: United kingdom