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Novel intron 2 polymorphism in the melanophilin gene is in Hardy-Weinberg equilibrium and is not associated with coat color in goats

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Open Journal of Genetics 2013年第3期3卷 195-200页

作者： Mufliat A. Adefenwa Brilliant O. Agaviezor Sunday O. Peters Matthew Wheto Oludotun J. Ekundayo Moses Okpeku Bola O. Oboh Khalid O. Adekoya Christian O. N. Ikeobi Marcos De Donato Bolaji N. Thomas Ikhide G. Imumorin Department of Animal Breeding and Genetics University of Agriculture Abeokuta Nigeria Department of Animal Science Cornell University Ithaca USA Department of Biomedical Sciences Rochester Institute of Technology Rochester USA Department of Cell Biology and Genetics University of Lagos Lagos Nigeria Department of Livestock Production Niger Delta University Amassomma Nigeria

Pigmentation plays important adaptation and physiological efficiency roles in animals. In the sequence of a 648 bp fragment representing intron 1, exon 2, and part of intron 2 of the MLPH mammalian pigmentation gene, we identified a novel g.469C> G mutation in intron 2, and genotyped it in 266 Nigerian goats using PCR-RFLP analysis. The C allele had frequencies of 0.9625, 0.9804 and 0.97405 in West African Dwarf (WAD),Sahel(SH) and Red Sokoto (RS) breeds, respectively. The G allele was the highest in WAD (0.0375), followed by RS (0.02595), and then SH (0.0196). Overall low FIS and FST and high Nm values demonstrate little differentiation within and among the goat breeds at this intronic locus. This g.469C> G polymorphism in MLPH gene is the first in any goat breed and also first in Nigerian goats. Our results suggest that this intronic SNP locus is maintained at Hardy-Weinberg equilibrium (P < 0.05) and the lack of association of this SNP with coat color may indicate its neutrality in goats.

关键词： Coat Color Goats melanophilin Nigeria Intron 2 SNP PCR-RFLP

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Myosin-5a motor function is co-activated by two cargo adaptor proteins RILPL2 and melanophilin

Myosin-5a motor function is co-activated by two cargo adapto...

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中国生物化学与分子生物学会2019年全国学术会议暨学会成立四十周年

作者： Qing-Juan Cao Ning Zhang Rui Zhou Lin-Lin Yao Xiang-dong Li Group of Cell Motility and Muscle Contraction State Key Laboratory of Integrated Management of Pest Insects and Rodents Institute of Zoology Chinese Academy of Sciences University of Chinese Academy of Sciences

Vertebrate myosin-5 a is an ATP-utilizing processive motor associated with the actin network and responsible for the transport and localization of several vesicle cargoes. To transport cargo efficiently and prevent futile ATP hydrolysis, myosin-5 a motor function must be tightly regulated. The globular tail domain(GTD) of myosin-5 a not only functions as the inhibitory domain, but also serves as the binding site for a number of cargo adaptor proteins, including melanophilin(Mlph) and Rab-interacting lysosomal proteinlike 2(RILPL2). In this study, using various biochemical approaches, including ATPase, single-molecule motility, and GST pulldown assays and analytical ultracentrifugation, we demonstrate that the binding of both Mlph and RILPL2 to the GTD of myosin-5 a is required for the activation of myosin-5 a motor function under physiological ionic conditions. We also found that this activation is regulated by the small GTPase Rab36, a binding partner of RILPL2. In summary, our results indicate that RILPL2 is required for Mlphmediated activation of Myo5 a motor activity under physiological conditions and that Rab36 promotes this activation. We propose that Rab36 stimulates RILPL2 to interact with the myosin-5 a GTD;this interaction then induces the exposure of the Mlph-binding site in the GTD, thereby enabling Mlph to interact with the GTD and activate myosin-5 a motor activity.

关键词： allosteric regulation melanophilin melanosome molecular motor myosin small GTPase vesicle transport

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