Biosynthetic production of fully carbon-13 labeled retinal in E. coli for structural and functional studies of rhodopsins

Munro, Rachel; Vlugt, Jeffrey de; Ward, Meaghan E.; Kim, So Young; Lee, Keon Ah; Jung, Kwang‐Hwan; Ladizhansky, Vladimir; Brown, Leonid S.

doi:10.1007/s10858-019-00225-9

Cited by 3 publications

(1 citation statement)

References 57 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Once recombinant DNA technology allowed the production of functional opsins in heterologous hosts, one could use this technology to adapt the intrinsic potential of opsins to one's need and design. Combining synthetic retinal design with Ganapathy et al (2015); Mei et al (2018); Ganapathy et al (2019); Hontani et al (2019); Munro et al (2019); Chuon et al (2021) Type-2 pigments: Arnaboldi et al (1979); Mollevanger et al (1987); Friedman et al (1989); Bhattacharya et al (1992b); Feng et al (1997); Huang et al (1997);DeLange et al (1998a); Iwasa et al (1998); Lugtenburg et al (1999); Verdegem et al (1999); Wada et al (2000); Spooner et al (2004); Wang et al (2004); Hirano et al (2006); Verhoeven et al (2006)…”

Section: Protein Joins Inmentioning

confidence: 99%

Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering

Grip

Ganapathy

2022

Front. Chem.

View full text Add to dashboard Cite

The first member and eponym of the rhodopsin family was identified in the 1930s as the visual pigment of the rod photoreceptor cell in the animal retina. It was found to be a membrane protein, owing its photosensitivity to the presence of a covalently bound chromophoric group. This group, derived from vitamin A, was appropriately dubbed retinal. In the 1970s a microbial counterpart of this species was discovered in an archaeon, being a membrane protein also harbouring retinal as a chromophore, and named bacteriorhodopsin. Since their discovery a photogenic panorama unfolded, where up to date new members and subspecies with a variety of light-driven functionality have been added to this family. The animal branch, meanwhile categorized as type-2 rhodopsins, turned out to form a large subclass in the superfamily of G protein-coupled receptors and are essential to multiple elements of light-dependent animal sensory physiology. The microbial branch, the type-1 rhodopsins, largely function as light-driven ion pumps or channels, but also contain sensory-active and enzyme-sustaining subspecies. In this review we will follow the development of this exciting membrane protein panorama in a representative number of highlights and will present a prospect of their extraordinary future potential.

show abstract