A distinct abundant group of microbial rhodopsins discovered using functional metagenomics

作者：Pushkarev Alina; Inoue Keiichi; Larom Shirley; Flores Uribe Jose; Singh Manish; Konno Masae; Tomida Sahoko; Ito Shota; Nakamura Ryoko; Tsunoda Satoshi P; Philosof Alon; Sharon Itai; Yutin Natalya; Koonin Eugene V; Kandori Hideki^*; Beja Oded^*

来源：Nature, 2018, 558(7711): 595-+.

DOI：10.1038/s41586-018-0225-9

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.

• 出版日期2018-6-28