Issue |
BIO Web Conf.
Volume 123, 2024
The 1st International Seminar on Tropical Bioresources Advancement and Technology (ISOTOBAT 2024)
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Article Number | 01025 | |
Number of page(s) | 7 | |
Section | Agriculture, Animal Sciences, Agroforestry, and Agromaritime Innovation | |
DOI | https://doi.org/10.1051/bioconf/202412301025 | |
Published online | 30 August 2024 |
Nucleotides Variability of Branched Chain Ketoacid Dehydrogenase E1-α Polypeptide (BCKDHA) Gene on Madura Cattle
1 Department of Biology, Faculty of Mathematics and Natural Sciences, IPB University, Bogor, Indonesia
2 Department of Biology, Faculty of Sciences, Institut Teknologi Sumatera, Lampung, Indonesia
* Corresponding author: witafar@apps.ipb.ac.id
Madura cattle is one of Indonesian native cattle which has physical strength and is highly adaptable under dry climates. Branched Chain α-Keto Dehydrogenase (BCKD) complex bound to mitochondrial inner membrane and catalyzes branched-chain amino acid catabolism into α-keto. Subunit E1-α of BCKD complex is encoded by the Branched Chain Ketoacid Dehydrogenase E1-α Polypeptide (BCKDHA) gene. This research was conducted to analyze the variability of the 3’ end promoter and exon 1 of the BCKDHA gene. Variant analysis was done on 8 samples of Madura cattle, 1 sample of filial Ongole cattle, and 1 sample of Bali cattle. Missense substitution was found in one sample of madura cattle, i.e. G95A that changed polypeptide, i.e. arginine to glutamine (Arg28Glu); other substitution was found in all samples, i.e. T125C and changed polypeptide; i.e. phenylalanine to serine (Phe38Ser). Several silent mutations on promoter and exon 1 were observed in all samples. Apart from the point mutation above, there was a six-base deletion (ATGGCG) in the exon 1 segment that was identified in 4 samples of Madura cattle that shortened two amino acids of the signal peptide of BCKDHA.
© The Authors, published by EDP Sciences, 2024
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