期刊
NATURE
卷 558, 期 7711, 页码 595-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41586-018-0225-9
关键词
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资金
- Israel Science Foundation - F.I.R.S.T. (Bikura) [545/17]
- I-CORE Program of the Planning and Budgeting Committee
- Grand Technion Energy Program (GTEP)
- Leona M. and Harry B. Helmsley Charitable Trust
- Weizmann Institute of Science
- Lorry I. Lokey Interdisciplinary Center for Life Sciences and Engineering
- Russell Berrie Nanotechnology Institute
- Louis and Lyra Richmond Memorial Chair in Life Sciences
- Japanese Ministry of Education, Culture, Sports, Science and Technology [26708001, 26115706, 26620005, 25104009, 15H02391]
- JST PRESTO [JPMJPR15P2, JPMJPR1688]
- JST CREST [JPMJCR1753]
Many organisms capture or sense sunlight using rhodopsin pigments(1,2), which are integral membrane proteins that bind retinal chromophores. Rhodopsins comprise two distinct protein families(1), type-1 (microbial rhodopsins) and type-2 (animal rhodopsins). The two families share similar topologies and contain seven transmembrane helices that form a pocket in which retinal is linked covalently as a protonated Schiff base to a lysine at the seventh transmembrane helix(2,3). Type-1 and type-2 rhodopsins show little or no sequence similarity to each other, as a consequence of extensive divergence from a common ancestor or convergent evolution of similar structures1. Here we report a previously unknown and diverse family of rhodopsins-which we term the heliorhodopsins-that we identified using functional metagenomics and that are distantly related to type-1 rhodopsins. Heliorhodopsins are embedded in the membrane with their N termini facing the cell cytoplasm, an orientation that is opposite to that of type-1 or type-2 rhodopsins. Heliorhodopsins show photocycles that are longer than one second, which is suggestive of light-sensory activity. Heliorhodopsin photocycles accompany retinal isomerization and proton transfer, as in type-1 and type-2 rhodopsins, but protons are never released from the protein, even transiently. Heliorhodopsins are abundant and distributed globally; we detected them in Archaea, Bacteria, Eukarya and their viruses. Our findings reveal a previously unknown family of light-sensing rhodopsins that are widespread in the microbial world.
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