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味觉特异性G蛋白α-味导素的功能表达。

Functional expression of the taste specific G-protein, alpha-gustducin.

作者信息

Hoon M A, Northup J K, Margolskee R F, Ryba N J

机构信息

Laboratory of Immunology, National Institute of Dental Research, N.I.H., Bethesda, MD 20892, USA.

出版信息

Biochem J. 1995 Jul 15;309 ( Pt 2)(Pt 2):629-36. doi: 10.1042/bj3090629.

DOI:10.1042/bj3090629
PMID:7626029
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1135777/
Abstract

The taste-specific G-protein alpha-subunit, alpha-gustducin, was expressed using a baculovirus based system. alpha-Gustducin was demonstrated to be myristoylated and was also palmitoylated in insect larval cells. Recombinant alpha-gustducin was purified to homogeneity. Neither receptors nor effectors that interact with gustducin in taste are known. However, alpha-gustducin has a close structural similarity to the visual G-protein, alpha-transducin. Therefore alpha-gustducin was reconstituted with components of the visual system to determine the degree of its functional similarity with alpha-transducin. Despite the fact that the sequences of alpha-gustducin and alpha-transducin share only 80% identity with each other, the interactions and functions of these two proteins were quantitatively identical. These included the interaction with receptor, bovine rhodopsin, with effector, bovine retinal cyclic GMP-phosphodiesterase, and with bovine brain and retinal G-protein beta gamma-heterodimers; receptor-catalysed GDP-GTP exchange and the intrinsic GTPase activity of alpha-gustducin and alpha-transducin were also identical. Gi alpha which is 70% identical with alpha-transducin interacts with different receptor and effector proteins and has very different guanine-nucleotide binding properties. Therefore, the functional equivalence of alpha-gustducin and alpha-transducin suggest that taste buds are likely to contain receptor and effector proteins that share many properties with their retinal equivalents.

摘要

利用杆状病毒表达系统表达了味觉特异性G蛋白α亚基α-味导蛋白。在昆虫幼虫细胞中，α-味导蛋白被证明发生了肉豆蔻酰化，也发生了棕榈酰化。重组α-味导蛋白被纯化至同质。目前尚不清楚味觉中与味导蛋白相互作用的受体和效应器。然而，α-味导蛋白与视觉G蛋白α-转导蛋白在结构上有密切的相似性。因此，将α-味导蛋白与视觉系统的组分重组，以确定其与α-转导蛋白功能相似的程度。尽管α-味导蛋白和α-转导蛋白的序列彼此仅具有80%的同一性，但这两种蛋白质的相互作用和功能在数量上是相同的。这些包括与受体牛视紫红质、效应器牛视网膜环鸟苷酸磷酸二酯酶以及与牛脑和视网膜G蛋白βγ异二聚体的相互作用；受体催化的GDP-GTP交换以及α-味导蛋白和α-转导蛋白的内在GTP酶活性也相同。与α-转导蛋白有70%同一性的Giα与不同的受体和效应器蛋白相互作用，并且具有非常不同的鸟嘌呤核苷酸结合特性。因此，α-味导蛋白和α-转导蛋白的功能等效性表明，味蕾可能含有与其视网膜对应物具有许多共同特性的受体和效应器蛋白。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08a3/1135777/ae2d07ee766c/biochemj00059-0264-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08a3/1135777/02d4aed878d0/biochemj00059-0261-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08a3/1135777/deea8dbac489/biochemj00059-0262-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08a3/1135777/d4710f3e8472/biochemj00059-0262-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08a3/1135777/ae2d07ee766c/biochemj00059-0264-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08a3/1135777/02d4aed878d0/biochemj00059-0261-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08a3/1135777/deea8dbac489/biochemj00059-0262-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08a3/1135777/d4710f3e8472/biochemj00059-0262-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/08a3/1135777/ae2d07ee766c/biochemj00059-0264-a.jpg

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