The Identification of Novel Single Nucleotide Polymorphisms in Calpain 1 (CAPN1) Gene of Japanese Quail (Coturnix coturnix japonica)
Öz
Objective: Calpains, in particular μ-calpain, are responsible for the post mortem proteolysis processes in muscle tissue and have main influences on meat quality. The CAPN1 gene that codes for large subunit of μ-calpain is revealed as a candidate gene related with meat quality and tenderization traits for livestock. For this reason, in this study it is aimed to investigate the genetic variation of CAPN1 gene in Japanese quails.
Material and Methods: In this study, the genetic variation of CAPN1 gene was analyzed via DNA sequencing of 35 (13 males and 12 females) Japanese quails which were reared in Tekirdağ Namık Kemal University, Animal Research Unit.
Results: Some genetic variants which are found in the 4th and 5th exons are as g.103969C>T in the 4th exon region and eight novel SNPs as g.104116A>T, g.104118T>G, g.104148G>C, g.104169G>C, g.104172A>G, g.104179C>G, g.104181G>A, g.104184T>C in the 5th exon of CAPN1 gene. The novel DNA polymorphisms of CAPN1 gene in Japanese quails are reported for the first time in this study and these sequences were deposited to NCBI GenBank Database, with the accession numbers MK496828-MK496837, respectively. g.103969C>T transversion which is localized in the 4th exon region and g.104148G>C, g.104169G>C transversions and g.104172A>G, g.104181G>A, g.104184T>C transitions which are localized in the 5th exon region have not caused an amino acid change. Instead, g.104116A>T, g.104118T>G tranversions caused the change from Threonine to Serine amino acid. Similarly, C→G transversion which was observed on the 104179th position caused the amino acid change from Proline to Alanine.
Conclusion: These observed SNPs may have an effect on meat yield and tenderness in quails, so further researches are needed to demonstrate this hypothesis and these SNPs may be candidate SNPs for quails breeding.
Anahtar Kelimeler
Kaynakça
- Barendse W. 2002. DNA markers for meat tenderness. Patent WO02064820. Bastos, pp. 1–88.
- Geesink GH, Koohmaraie M. 1999. Effect of calpastatin on degradation of myofibrillar proteins by l-calpain under postmortem conditions. Journal of Animal Science 77: 2685–2692.
- Goll, D.E., Thompson, V.F., Li, H.,Wei,W., Cong, J., 2003. The calpain system. Physiological Reviews 83: 731–801
- Hall T. 2011. BioEdit: An important software for molecular biology. GERF Bulletin of Biosciences 2(1):60-61.
- Ishiura S, Murofushi H, Suzuki K, Imahori K. 1978. Study of a calcium-activated neutral protease from chicken skeletal muscle. The Journal of Biological Chemistry 84: 225–230.
- Koohmaraie M. 1992. The role of Ca(2+)-dependent proteases (calpains) in post mortem proteolysis and meat tenderness. Biochimie 74: 239–245.
- Koohmaraie M, Geesink GH. 2006. Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. Meat Science 74: 34–43.
- Geesink GH, Koohmaraie M. 1999. Postmortem Proteolysis and Calpain/Calpastatin Activity in Callipyge and Normal Lamb Biceps Femoris During Extended Postmortem Storage. Journal of Animal Science 77:1490-1501.
- Johari S, Maeda Y, Okamoto S, Hashiguchi T. 1993. Comparison of calpain and calpastatin activities in skeletal muscle of broiler and layer chickens. British Poultry Science 34: 819–824.
- Li Z, Cao B, Zhao B, Yang X, Fan MZ, Yang J. 2009. Decreased expression of calpain and calpastatin mRNA during development is highly correlated with muscle protein accumulation in neonatal pigs. Comparative Biochemistry and Physiology - Part A: Molecular & Integrative Physiology 152: 498–503.