Identification and characterization of a third thioredoxin h in poplar |
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| Institution: | 1. Interactions Arbres-Micro-organismes INRA, Faculté des Sciences, Université H. Poincaré-Nancy I (UMR 1136), 54506 Vandoeuvre-les-Nancy, France;2. Department of Medical Biochemistry and Biophysics, Karolinska Institute, Medical Nobel Institute for Biochemistry, 171 77 Stockholm, Sweden;3. Laboratoire des BioSciences de l’Aliment INRA, Faculté des Sciences, Université H. Poincaré-Nancy I, (UC885), 54506 Vandoeuvre-les-Nancy, France;4. Laboratoire d’Endocrinologie des Annélides, Université des Sciences et Technologies de Lille (UPRESA 8017), 59655 Villeneuve d’Ascq cedex, France;1. Department of Marine Life Sciences, School of Marine Biomedical Sciences, Jeju National University, Jeju Self-Governing Province 690-756, Republic of Korea;2. Fish Vaccine Research Center, Jeju National University, Jeju Special Self-Governing Province 695-965, Republic of Korea;3. New Strategy Research Center, National Fisheries Research and Development Institute, Busan 619-705, Republic of Korea;1. State Key Laboratory of Tree Genetics and Breeding, Chinese Academy of Forestry, Beijing, 100091, China;2. Umeå Plant Science Centre, Department of Plant Physiology, Umeå University, SE-901 87, Umeå, Sweden;1. College of Landscape Architecture, Sichuan Agricultural University, Chengdu, 611130, China;2. Institute of Landscape Architecture, Sichuan Agricultural University, Chengdu, 611130, China;3. Sichuan Tianyi Ecological Garden Group Co. LTD, Chengdu, 610041, China;4. Sichuan Normal University, Chengdu, 610101, China;5. Sichuan Agricultural University, Chengdu, 611130, China;1. Department of Hepatobiliary and Pancreatic Surgery, The First Affiliated Hospital of Zhengzhou University; Henan Key Laboratory of Digestive Organ Transplantation; Zhengzhou Key Laboratory of Hepatobiliary & Pancreatic Diseases and Organ Transplantation; Open and Key Laboratory of Hepatobiliary & Pancreatic Surgery and Digestive Organ Transplantation at Henan Universities; Zhengzhou, 450001, China;2. Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203, China;3. School of Life Science and Medicine, Dalian University of Technology, Panjin, 124221, China;4. Dalian Runsheng Kangtai Medical Laboratory Co.Ltd, Dalian, China;1. Division of Applied Life Science (BK21Plus), PMBBRC & IALS, Gyeongsang National University, Jinju 660-701, Republic of Korea;2. College of Pharmacy and Research Institute of Pharmaceutical Science, PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea |
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| Abstract: | Three full-length sequences encoding thioredoxin h have been isolated in a leaf/root of Populus trichocarpa cv. Trichobel expressed sequence tag (EST) library. One of these, popCXXS1 exhibits the nontypical active site CXXS homologous to atCXXS1. The second one, named popTrxh4, is related to atTrxh9 which forms with several other plant thioredoxin h a distinct subgroup of thioredoxins h. The third one, named popTrxh3, displays 66% identity and also a high degree of homology (81%) vs. the previously described popTrxh1. Nevertheless, the active sites of both proteins differ, since the active site of popTrxh1 (WCPPC) is a variant of the canonical WCGPC found in popTrxh3. The cDNA sequence of popTrxh3 has been introduced in an expression plasmid (pET3d) in order to express the corresponding recombinant polypeptide. The protein has been expressed to a high level, purified from Escherichia coli cells with a high yield and its catalytic properties compared to popTrxh1. Furthermore, two mutants, popTrxh1P40G and popTrxh3G41P, have been engineered in order to explore the importance of the active site residues in the thioredoxin h catalytic properties. The results are discussed in relation with known biochemical properties of thioredoxins h. |
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