Melanophilin polymorphism in ferrets of different colors

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In mammals, the main contribution to the variability of pigmentation is made by two groups of genes directly related to the metabolic pathways of pigment synthesis and controlling the transport of melanosomes in melanocytes to keratinocytes. In order to identify the genetic basis of pigmentation variants, the nucleotide sequences of the melanophilin gene were compared in two groups of ferrets – silver-colored and wild-type animals using sequencing of 16 exons. In carriers of silver color, a single nucleotide deletion was detected in the 9th exon, leading to a shift in the reading frame and the formation of a stop codon downstream. The protein encoded by the mutant allele is almost completely devoid of the C terminal domain of the protein responsible for the contact of melanosomes with actin during their muving to the periphery of melanocytes, but it retains the leading domain involved in the formation of melanosomes. The combination of the preservation of the N domain and the defect of the C domain of the mutant protein for the first time makes it possible to explain the incomplete dominance of the wild-type protein in heterozygotes.

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G. Kosovsky

Afanas’ev Research Institute of Fur-Bearing Animal Breeding and Rabbit Breeding

编辑信件的主要联系方式.
Email: gkosovsky@mail.ru

Corresponding Member of the RAS

俄罗斯联邦, pos. Rodniki, Ramenskii Region, Moscow Province

V. Glazko

Afanas’ev Research Institute of Fur-Bearing Animal Breeding and Rabbit Breeding

Email: gkosovsky@mail.ru
俄罗斯联邦, pos. Rodniki, Ramenskii Region, Moscow Province

O. Abramov

Afanas’ev Research Institute of Fur-Bearing Animal Breeding and Rabbit Breeding

Email: gkosovsky@mail.ru
俄罗斯联邦, pos. Rodniki, Ramenskii Region, Moscow Province

T. Glazko

Afanas’ev Research Institute of Fur-Bearing Animal Breeding and Rabbit Breeding

Email: gkosovsky@mail.ru
俄罗斯联邦, pos. Rodniki, Ramenskii Region, Moscow Province

参考

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2. Fig. 1. The sequence chromatogram containing the mutation was obtained. A similar section of the mlph gene in a wild–type ferret is shown above, and a mutant type is shown below (highlighted with a rectangle).

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3. Fig. 2. Comparison of amino acid sequences of wild and mutant forms of melanophilin. For clarity, we have highlighted the amino acid sequences of the two forms that are identical in green, and those that differ in yellow and italics. The first modified amino acid is also highlighted with an underscore.

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4. Fig. 3. The structure of wild-type melanophilin. The binding domain to the Rab27A protein is highlighted in a circle on the left. Further along the sequence, there are two alpha chains. The first of them belongs to the myosin binding domain, the second is part of the functional actin binding domain. The mutation point present in a similar sequence of a mutant protein is marked with an arrow.

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5. Fig. 4. The structure of melanophilin of the mutant type. The Rab27a protein binding domain is highlighted in a circle. The mutant amino acid is marked with an arrow. The sequence of amino acids after the mutation point does not correspond to a similar sequence in the wild type. The two alpha chains present in this figure are not analogous to the alpha chains in the wild-type protein.

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