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• W201458029 abstract "Membrane proteins present unparalleled challenges for structural biology initiatives, nascent functional genomics efforts, and drug discovery experiments. To obtain sufficient quantities of membrane proteins for these studies, an expression system based upon the Rhodobacter species of photosynthetic bacteria is being employed. This system exploits this organism's unique physiology whereby strongly induced heterologous expression of target membrane proteins can be coordinated with synthesis of new membranes, thereby favoring membrane insertion of natively folded polypeptides. A series of vectors utilizing promoters responding to oxygen and/or light has been constructed. A variety of engineered host strains is available that carry deletions of one or more native transmembrane complexes, thereby increasing the membrane volume available for the accommodation of foreign protein. Using this approach, data suggest that many target membrane proteins from a variety of organisms can be produced and purified at levels that equal or exceed those of native membrane protein complexes (10 mg/l). Standardized strategies have been developed for semiautomation of cloning and purification. An analysis of nearly 500 expression strains (including representatives encompassing an entire membrane proteome) has shown that ∼60% of the membrane proteins are expressed in Rhodobacter at levels that exceed 1 mg/l of cell culture (many at levels of 10‐20 mg/l) are localized within intracytoplasmic membranes (ICMs), and—most importantly—display structural and functional integrity. The Rhodobacter system represents an advance towards the development of an integrated strategy for obtaining structures of this important class of proteins at a more rapid pace." @default.
• W201458029 created "2016-06-24" @default.
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• W201458029 date "2009-01-01" @default.
• W201458029 modified "2023-10-16" @default.
• W201458029 title "Chapter 3 Harnessing Photosynthetic Bacteria for Membrane Protein Production" @default.
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• W201458029 doi "https://doi.org/10.1016/s1063-5823(09)63003-9" @default.
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