Hostname: page-component-cd9895bd7-q99xh Total loading time: 0 Render date: 2024-12-24T18:50:00.307Z Has data issue: false hasContentIssue false

Comparative genomics of casein genes

Published online by Cambridge University Press:  24 July 2019

Moses Madende*
Affiliation:
Department of Microbial, Biochemical and Food Biotechnology, University of the Free State, PO Box 339, Bloemfontein 9301, Republic of South Africa
Gernot Osthoff
Affiliation:
Department of Microbial, Biochemical and Food Biotechnology, University of the Free State, PO Box 339, Bloemfontein 9301, Republic of South Africa
*
Author for correspondence: Moses Madende, Email: [email protected]

Abstract

This research paper addresses the hypothesis that comparative genomics can give a new insight into the functionality of casein genes with respect to the casein micelle. Comparative genomics is a rapidly emerging field in computational biology whereby two or more genomes are compared in order to obtain a global view on genomes as well as assigning previously unknown functions for genes. Casein genes are among the most rapidly evolving mammalian genes, with the gene products mainly grouped into four types (αs1-, αs2-, β- and κ-casein). Functionally, casein genes are central to the casein micelle, the exact structure of which is still a subject of intense debate. Moreover, and adding to this complexity, some mammals lack some of the casein genes, although casein micelles have been observed in their milk. This observation has prompted an investigation into the distribution of casein genes across a host of mammalian species. It was apparent from this study that casein gene sequences are very diverse from each other and we confirmed that many mammalian species lack one or more of the casein genes. The genes encoding β- and κ-caseins are present in most mammals whereas α-casein encoding genes are less represented. This suggests different mechanisms for casein micelle formation in different species as well as the functions that are assigned to each individual casein.

Type
Research Article
Copyright
Copyright © Hannah Dairy Research Foundation 2019 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Aken, BL, Achuthan, P, Akanni, W, et al. (2017) Ensembl 2017. Nucleic Acids Research 45, D635D642.Google Scholar
Di Palma, F, Alfoldi, J, Johnson, J, Berlin, A, Gnerre, S, Jaffe, D, MacCallum, I, Young, S, Walker, BJ and Lindblad-Toh, K (2011) The Draft Genome of Spermophilus tridecemlineatus Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.Google Scholar
Ginger, MR and Grigor, MR (1999) Comparative aspects of milk caseins. Comparative Biochemistry and Physiology Part B 124, 133145.Google Scholar
Herrero, J, Muffato, M, Beal, K, et al. (2016) Ensembl comparative genomics resources. Database 2016, bav096. doi: 10.1093/database/bav096Google Scholar
Holt, C (2015) Casein and casein micelle structures, functions and diversity in 20 species. International Dairy Journal 60, 213.Google Scholar
Holt, C, Carver, JA, Ecroyd, H and Thorn, DC (2013) Invited review: caseins and the casein micelle: their biological functions, structures, and behavior in foods. Journal of dairy science 96, 61276146.Google Scholar
Horne, DS (1998) Casein interactions: casting light on the black boxes, the structure in dairy products. International Dairy Journal 8, 171177.Google Scholar
Kawasaki, K, Lafont, AG and Sire, JY (2011) The evolution of milk casein genes from tooth genes before the origin of mammals. Molecular Biology and Evolution 28, 20532061.Google Scholar
Koonin, EV (2005) Orthologs, paralogs, and evolutionary genomics. Annual Review of Genetics 39, 309338.Google Scholar
Madende, M, Osthoff, G, Patterton, H, et al. (2015) Characterization of casein and alpha lactalbumin of African elephant (Loxodonta africana) milk. Journal of Dairy Science 98, 83088318.Google Scholar
Madende, M, Kemp, G, Stoychev, S and Osthoff, G (2018) Characterisation of African elephant beta casein and its relevance to the chemistry of caseins and casein micelles. International Dairy Journal 85, 112120.Google Scholar
Martin, P, Cebo, C and Miranda, G (2013) Interspecies comparison of milk proteins: quantitative variability and molecular diversity. In McSweeney, P and Fox, P (eds.), Advanced Dairy Chemistry: Volume 1A: Proteins: Basic Aspects, 4th Edn., Boston, MA: Springer, pp. 387429.Google Scholar
Muller, H, Naumann, F and Freytag, J-C (2003) Data Quality in Genome Databases. In: Proceedings of the Conference on Information Quality. pp. 269284.Google Scholar
Phadungath, C (2005) Casein micelle structure: a concise review. Journal of Science and Technology 27, 201212.Google Scholar
Rijnkels, M, Elnitski, L, Miller, W and Rosen, JM (2003) Multispecies comparative analysis of a mammalian-specific genomic domain encoding secretory proteins. Genomics 82, 417432.Google Scholar
Rollema, HS (1992) Casein association and micelle formation. In Fox, PF (ed.), Advanced Dairy Chemistry, Vol. 1: Proteins. Essex: Elsevier Science Publisher, Ltd., pp. 111140.Google Scholar
Smyth, E, Clegg, RA and Holt, C (2004) A biological perspective on the structure and function of caseins and casein micelles. International Journal of Dairy Technology 57, 121126.Google Scholar
Walstra, P and Jenness, R (1984) Dairy Chemistry and Physics. New York: Wiley. 467Google Scholar
Wei, L, Liu, Y, Dubchak, I, et al. (2002) Comparative genomics approaches to study organism similarities and differences. Journal of Biomedical Informatics 35, 142150.Google Scholar
Wong, NP (1988) Fundamental of Dairy Chemistry, 3rd Edn. New York: Van Nostrand Reinhold, pp. 481492.Google Scholar
Supplementary material: PDF

Madende and Osthoff supplementary material

Madende and Osthoff supplementary material 1

Download Madende and Osthoff supplementary material(PDF)
PDF 491 KB