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Article|01 Apr 2018|OPEN
Identification and substrate prediction of new Fragaria x ananassa aquaporins and expression in different tissues and during strawberry fruit development
Britt Merlaen1 , , Ellen De Keyser2 and Marie-Christine Van Labeke,1 ,
1Plant Production, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, 9000 Gent, Belgium
2Flanders Research Institute for Agriculture Fisheries and Food (ILVO), Plant Sciences Unit, Caritasstraat 39, 9090 Melle, Belgium
*Corresponding author. E-mail: britt.merlaen@ugent.be,mariechristine.vanlabeke@ugent.be

Horticulture Research 5,
Article number: 20 (2018)
doi: https://doi.org/10.1038/s41438-018-0019-0
Views: 955

Received: 10 Aug 2017
Revised: 15 Dec 2017
Accepted: 11 Jan 2018
Published online: 01 Apr 2018

Abstract

The newly identified aquaporin coding sequences presented here pave the way for further insights into the plant–water relations in the commercial strawberry (Fragaria x ananassa). Aquaporins are water channel proteins that allow water to cross (intra)cellular membranes. In Fragaria x ananassa, few of them have been identified hitherto, hampering the exploration of the water transport regulation at cellular level. Here, we present new aquaporin coding sequences belonging to different subclasses: plasma membrane intrinsic proteins subtype 1 and subtype 2 (PIP1 and PIP2) and tonoplast intrinsic proteins (TIP). The classification is based on phylogenetic analysis and is confirmed by the presence of conserved residues. Substrate-specific signature sequences (SSSSs) and specificity-determining positions (SDPs) predict the substrate specificity of each new aquaporin. Expression profiling in leaves, petioles and developing fruits reveals distinct patterns, even within the same (sub)class. Expression profiles range from leaf-specific expression over constitutive expression to fruit-specific expression. Both upregulation and downregulation during fruit ripening occur. Substrate specificity and expression profiles suggest that functional specialization exists among aquaporins belonging to a different but also to the same (sub)class.