| Title: | Helicoverpa-inducible Thioredoxin h from Cicer arietinum: structural modeling and potential targets |
| Author(s): | Singh A; Tyagi C; Nath O; Singh IK; |
| Address: | "Department of Botany, Hans Raj College, University of Delhi, Delhi, 110007, India. Department of Microbiology, University of Szeged, Kozep fasor 52., 6726, Szeged, Hungary. Molecular Biology Research Laboratory, Deshbandhu College, University of Delhi, Kalkaji, New Delhi, 110019, India. Molecular Biology Research Laboratory, Deshbandhu College, University of Delhi, Kalkaji, New Delhi, 110019, India; Department of Entomology, University of Kentucky, S-225 AG. Science, North, Lexington, KY 40546-0001, United States. Electronic address: iksingh@db.du.ac.in" |
| DOI: | 10.1016/j.ijbiomac.2017.12.079 |
| ISSN/ISBN: | 1879-0003 (Electronic) 0141-8130 (Linking) |
| Abstract: | "Thioredoxins are small and universal proteins, which are involved in the cell redox regulation. In plants, they participate in a broad range of biochemical processes like self-incompatibility, seed germination, pathogen & pest defense and oxidative stress tolerance. The h-type of thioredoxin (Trx-h) protein represents the largest Trx family. Herein, we characterized the Helicoverpa - inducible Trx h from an important legume, Cicer arietinum, CaHaTrx-h, 'CGFS' type Trxs, which encodes for a 113 amino acids long protein and possess characteristic motifs 'FLKVDVDE' and 'VVDFTASWCGPCRFIAPIL' and 73% sequence identity with AtTrx-h. Homology modeling and simulation of the target showed that the extended ss-sheet regions remain stable during the simulation while the helical regions fluctuate between alpha and 3-(10) helical forms and highlights the flexibility of helix2-helix3 and terminal regions probably to accommodate an approaching protein target and facilitate their interaction. During the simulation, the structure exists in five energy minima clusters with biggest cluster size belonging to 20-25?ª+ns time frames. PR-5 and Mannitol Dehydrogenase were nominated as potential targets and share close interaction with CaHaTrx-h via disulfide bond reduction. The study is an effort in the direction of understanding stress-related mechanisms in crop plants to overcome losses in agricultural yield" |
| Keywords: | "Amino Acid Sequence Base Sequence Catalytic Domain Cicer/chemistry/*genetics/metabolism Gene Expression Regulation, Plant Gene Regulatory Networks *Herbivory Models, Molecular Oxidation-Reduction Phylogeny Protein Conformation Reproducibility of Results S;" |
| Notes: | "MedlineSingh, Archana Tyagi, Chetna Nath, Onkar Singh, Indrakant K eng Netherlands 2017/12/21 Int J Biol Macromol. 2018 Apr 1; 109:231-243. doi: 10.1016/j.ijbiomac.2017.12.079. Epub 2017 Dec 17" |
