Structural characterizations of peroxisomal ABC transporter Pxa1p in Saccharomyces cerevisiae / 酵母菌過氧化體ABC運輸蛋白Pxa1p的結構特性分析

碩士 / 中山醫學大學 / 生化暨生物科技研究所 / 96 / ATP-binding cassette (ABC) transporters are members of a superfamily of membrane proteins involved in the transport of a variety of molecules across biological membranes. So far, four ABC transporters have been detected in mammalian peroxisomes, one of which, named ALDP, is specifically involved in the β-oxidation of the very long chain fatty acid. The marked genetic disorder ALD (adrenoleukodystrophy) was due to the mutation of the ALDP gene. It have been demonstrated that ALDP forms the homo-complex by itself and hetero-complex with other two peroxisomal ABC transporters via its C-terminal domain. In yeast, there are two orthologs of ALDP and PMP70 with the name of Pxa1p and Pxa2p, respectively. The results from biochemical and genetic studies have suggest that Pxa1p/Pxa2p can form hetero-dimers. However, the possibilities of the homo-dimer formation by Pxa1p/Pxa2p have not been excluded with certainty. So, we prepare the recombinant Pxa1pC-HA protein, containing C-terminal domain of Pxa1p, and use gel-filtration to determine its molecular weights. From the calculations of the molecular weights, we found that Pxa1pC-HA can form homo-complex composed of 2~4 monomers. Based on this study, we speculate full-length Pxalp may form homo-complex as Pxa1pC-HA.

Identiferoai:union.ndltd.org:TW/096CSMU5107028
Date January 2008
CreatorsJie-Mau, 黃傑懋
ContributorsRong-Tzong Tsai, 蔡榮宗
Source SetsNational Digital Library of Theses and Dissertations in Taiwan
Languagezh-TW
Detected LanguageEnglish
Type學位論文 ; thesis
Format66

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