Zinc is an important catalytic element for more than 300 enzymes and plays a structural role in the stabilization of many proteins. Protein domain analysis showed that identified Zn transporter proteins belong to the ZIP protein family (PF02535). | Turkish Journal of Biology Turk J Biol (2016) 40: 600-611 © TÜBİTAK doi: Research Article Comparative and phylogenetic analysis of zinc transporter genes/proteins in plants 1 1 2, Recep VATANSEVER , İbrahim İlker ÖZYİĞİT , Ertuğrul FİLİZ * Department of Biology, Faculty of Science and Arts, Marmara University, İstanbul, Turkey 2 Department of Crop and Animal Production, Çilimli Vocational School, Düzce University, Düzce, Turkey 1 Received: Accepted/Published Online: Final Version: Abstract: Zinc is an important catalytic element for more than 300 enzymes and plays a structural role in the stabilization of many proteins. Protein domain analysis showed that identified Zn transporter proteins belong to the ZIP protein family (PF02535). Zn transporter sequences were found to have similar molecular weights (– kDa) and amino acid lengths (306–478 amino acids) with – pI values. Subcellular localization of Zn transporters was predicted as the plasma membrane. They had 6–9 putative transmembrane domains with a variable region between TM-3 and TM-4, which could contain a potential histidine-rich metal-binding domain. Moreover, alignment analysis showed that the TM-2, -4, and -5 domains could be potential metal-binding sites because they contain highly conserved His residues. Based on a homology search, the retrieved sequences were identified as corresponding homologs of either Arabidopsis thaliana or Oryza sativa. Phylogenetic analysis also supported that A. thaliana and O. sativa sequences could be used as a reference/benchmark to identify Zn transporter homologs in various plant species. The findings of this study will be valuable theoretical knowledge for feature studies in terms of understanding the gene and protein features of Zn transporters in various plants. Key words: ZIP, transmembrane domain, histidine residue, metal-binding site, conserved .
