Genetic and structural characterization of the growth hormone gene and protein from tench, Tinca tinca.
The analysis of the tench growth hormone gene structure revealed a comparable organization of coding and non-coding regions than other from cyprinid species. Based on the performed mRNA and amino acid sequence alignments, gh tench is related to Asian than to European representatives of Cyprinidae family. Second aim of the work was to characterize and predict protein structure of the tench growth hormone. Tinca tinca GH share many common features with human GH molecule. The Tench GH protein binds to the growth hormone receptor (GHR) using two regions I and II that are situated at opposite sites of molecule. Binding site I is placed in the central part of T. tinca GH and H 189 amino acid in the middle region of the IV helix is crucial for GH-GHR interactions.
Department of Aquaculture, West Pomeranian University of Technology, Szczecin, Kazimierza Krolewicza 4, 71-550, Szczecin, Poland. rpanicz@zut.edu.pl.
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R
Panicz
Department of Aquaculture, West Pomeranian University of Technology, Szczecin, Kazimierza Krolewicza 4, 71-550, Szczecin, Poland.
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J
Sadowski
Department of Immunology, Microbiology and Physiological Chemistry, West Pomeranian University of Technology, Szczecin, Doktora Judyma 24, 71-466, Szczecin, Poland.
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R
Drozd
D000818:Animals; D001483:Base Sequence; D003530:Cyprinidae / Q000378:metabolism*; D004247:DNA / Q000235:genetics; D005786:Gene Expression Regulation / Q000502:physiology; D013006:Growth Hormone / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation
D013006:Growth Hormone; D004247:DNA