Molybdenum cofactor sulfurases (MCSUs) are important enzymes for plant development and response to environmental queues, including processes such as nitrogen metabolism and regulation of the abscisic acid levels in plant tissues. | Turkish Journal of Agriculture and Forestry Research Article Turk J Agric For (2015) 39: 786-796 © TÜBİTAK doi: Barley molybdenum cofactor sulfurase (MCSU): sequencing, modeling, and its comparison to other higher plants Ertuğrul FİLİZ1, Assaf DISTELFELD2, Tzion FAHIMA3, Özge KARAKAŞ METİN4, Eviatar NEVO3, Song WEINING5, Ahu ALTINKUT UNCUOĞLU6,* 1 Department of Crop and Animal Production, Çilimli Vocational School, Düzce University, Düzce, Turkey 2 Department of Molecular Biology and Ecology of Plants, Tel Aviv University, Tel Aviv, Israel 3 Institute of Evolution, University of Haifa, Haifa, Israel 4 TÜBİTAK, Marmara Research Center, Genetic Engineering and Biotechnology Institute, Kocaeli, Turkey 5 Northwest A&F University, State Key Laboratory of Crop Stress Biology for the Arid Areas College of Agronomy, Shaanxi, China 6 Department of Bioengineering, Faculty of Engineering, Marmara University, İstanbul, Turkey Received: Accepted/Published Online: Printed: Abstract: Molybdenum cofactor sulfurases (MCSUs) are important enzymes for plant development and response to environmental queues, including processes such as nitrogen metabolism and regulation of the abscisic acid levels in plant tissues. We cloned and sequenced MCSU gene from barley and performed in silico comparison with rice, tomato, and Arabidopsis. Physico-chemical properties and subcellular predictions were found to be similar in different plant species. All MCSUs had three critical domains: aminotransferase class-V (Pfam: PF00266), MOSC N-terminal beta barrel (Pfam: PF03476), and MOSC (Pfam: PF03473). Secondary structure analysis revealed that random coils were the most abundant, followed by α-helices and extended strands. Predicted binding sites of MCSUs were different in barley and Arabidopsis, whereas rice and tomato showed the same pattern. A conserved triple-cysteine motif was detected in all .
