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Directional Self-assembly in archaerhodopsin-Reconstituted Phospholipid Liposomes

Chinese Journal of Chemistry 2005年第3期23卷 330-333页

作者：吴佳黄力刘坚明明李庆国丁建东 DepartmentofMacromolecularScience KeyLaboratoryofMolecularEngineeringofPolymersFudanUniversityShanghai200433China DepartmentofPhysiologyandBiophysics SchoolofLifeSciencesFudanUniversityShanghai200433China

This paper reports, for the first time, that archaerhodopsin‐4 (AR4) could be reconstituted into phospholipid liposomes by self‐assembly. AR4 is a new membrane protein isolated from halobacteria H. sp . xz515 in a salt lake of Tibet, China. This is a bacteriorhodopsin (bR) like protein, function as a light‐driven proton pump. Experimental measurements verified that similar to bR, AR not only remains its biological activity in proteoliposome, but also keeps a preferred orientation in self‐assembly.

关键词： self‐assembly proteoliposome archaerhodopsin bacteriorhodopsin orientation

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Primary structure of helix C to helix G of a new retinal protein in ***515

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Chinese Science Bulletin 2000年第12期45卷 1108-1113页

作者： Hui Wang Shuxuan Zhan Qingan Sun Deqiang Xu Wei Zhao Weida Huang Qingguo Li Fudan Univ Sch Life Sci Shanghai 200433 Peoples R China

The gene fragment encoding the retinal protein from helix C to helix G in a new strain of halobacteria, ***515 has been amplified by PCR method. The nucleotide sequence of this fragment has been determined. The deduced amino acid sequence has been compared with halobium br and other two br-like proteins, ar-1 and ar-2. Results show that those amino acid residues in br, essential for proton pumping and binding to retinal, are conserved. The residue M145 in br may be important for isomerization reaction of retinal.

关键词： halohactcria claret membrane archaerhodopsin PCR sequence.

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Imaging bacteriorhodopsin-like molecules of claret-membranes from Tibet halobacteria xz515 by atomic force microscope

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Chinese Science Bulletin 2001年第22期46卷 1897-1900页

作者： TANG Lin SUN Qing’an LI Qingguo HUANG Yibo WEI Qingqing ZHANG Yi HU Jun ZHANG Zhihong LI Minqian YANG Fujia Laboratory of Detection and Manipulation of Single Molecule Shanghai Institute of Nuclear ResearchChinese Academy of SciencesShanghai 201800China Liren Laboratory Department of Physiology and BiophysicsSchool of Life SciencesFudan UniversityShanghai 200433China Laboratory of Neurobiology Shanghai Institute of PhysiologyChinese Academy of SciencesShanghai 200031China Moden Institute of Physics Fudan UniversityShanghai 200433China Center for Bio-X Science Study Shanghai Jiao Tong UniversityShanghai 200030China

Halobacteria *** 515 was isolated from a salt lake in Tibet. Although proton release-and-uptake across claret membrane is in reverse order compared to bacteri-orhodopsin in purple membrane from Halobacterium Sali-narum, and its efficiency of proton pump is much lower, AFM image shows that the molecules are still arranged in a two-dimensional hexagonal lattice of trimers. Primary structure of C- to G-helix of the archaerhodopsin shows that it has only 56% homology with bacteriorhodopsin. But the interactive amino acid residues at the interface between B-and D-helixes are conserved. These amino acid residues are believed to play a significant role in the stability of protein oligomers.

关键词： atomic force microscope archaerhodopsin bacteri- orhodopsin hexagonal lattice halobacteria.

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