Harris Nicola J, Booth Paula J
School of Biochemistry, University of Bristol, UK.
Biochim Biophys Acta. 2012 Apr;1818(4):1055-66. doi: 10.1016/j.bbamem.2011.11.006. Epub 2011 Nov 11.
Transmembrane transporters are responsible for maintaining a correct internal cellular environment. The inherent flexibility of transporters together with their hydrophobic environment means that they are challenging to study in vitro, but recently significant progress been made. This review will focus on in vitro stability and folding studies of transmembrane alpha helical transporters, including reversible folding systems and thermal denaturation. The successful re-assembly of a small number of ATP binding cassette transporters is also described as this is a significant step forward in terms of understanding the folding and assembly of these more complex, multi-subunit proteins. The studies on transporters discussed here represent substantial advances for membrane protein studies as well as for research into protein folding. The work demonstrates that large flexible hydrophobic proteins are within reach of in vitro folding studies, thus holding promise for furthering knowledge on the structure, function and biogenesis of ubiquitous membrane transporter families. This article is part of a Special Issue entitled: Protein Folding in Membranes.
跨膜转运蛋白负责维持细胞内正确的环境。转运蛋白固有的灵活性及其疏水环境意味着在体外研究它们具有挑战性，但最近已取得显著进展。本综述将聚焦于跨膜α螺旋转运蛋白的体外稳定性和折叠研究，包括可逆折叠系统和热变性。还描述了少数ATP结合盒转运蛋白的成功重新组装，因为这在理解这些更复杂的多亚基蛋白的折叠和组装方面是向前迈出的重要一步。这里讨论的转运蛋白研究代表了膜蛋白研究以及蛋白质折叠研究的重大进展。这项工作表明，大型柔性疏水蛋白已能够进行体外折叠研究，因此有望进一步了解普遍存在的膜转运蛋白家族的结构、功能和生物发生。本文是名为“膜中的蛋白质折叠”的特刊的一部分。
