RHO Membrane Protein Introduction

Introduction of RHO

Rhodopsin (also known as visual purple), encoded by RHO gene, is a light-sensitive receptor protein involved in visual phototransduction. It was discovered by Franz Christian Boll in 1876 and was named after ancient Greek ῥόδον (rhódon) for "rose", due to its pinkish color, and ὄψις (ópsis) for "sight". Rhodopsin is a biological pigment discovered from the rods of the retina. It is also a G-protein-coupled receptor (GPCR). Rhodopsin is significantly sensitive to light, helping vision in low-light conditions. When exposed to light, rhodopsin immediately photobleaches. In humans, rhodopsin is regenerated fully in about 30 minutes.

Basic Information of RHO
Protein Name	Rhodopsin
Gene Name	RHO
Aliases	Opsin-2
Organism	Homo sapiens (Human)
UniProt ID	P08100
Transmembrane Times	7
Length (aa)	348
Sequence	MNGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNNESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWVPYASVAFYIFTHQGSNFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTTICCGKNPLGDDEASATVSKTETSQVAPA

Function of RHO Membrane Protein

Rhodopsin is an important G-protein coupled receptor in phototransduction. Mutation of the rhodopsin gene mainly contributes to various retinopathies such as retinitis pigmentosa. Generally speaking, the protein related to the disease can aggregate with ubiquitin in inclusion bodies, destroy the intermediate filament network, and make up the ability of the cell to degrade non-functioning proteins, which leads to photoreceptor apoptosis. Other mutations in this gene can lead to X-linked congenital stationary night blindness via constitutive activation, especially when the mutations occur around the chromophore binding pocket of rhodopsin. Several other pathological states brought by rhodopsin have also been figured out, including poor post-Golgi trafficking, dysregulated activation, rod outer segment instability, and arrestin binding.

RHO Membrane Protein Introduction Fig. 1 3D structure of bovine rhodopsin.

Application of RHO Membrane Protein in Literature

Farrens D.L., et al. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science. 1996, 274(5288):768-70. PubMed ID: 8864113

The article finds that activation of transducin can be prevented by disulfide cross-linking of the helices, which in further suggests the importance of this movement for activation of rhodopsin.
Béjà O., et al. Bacterial rhodopsin: evidence for a new type of phototrophy in the sea. Science. 2000, 289(5486):1902-6. PubMed ID: 10988064

This article demonstrates that archaeal-like rhodopsins are broadly distributed among different taxa. It also indicates that the mode of bacterially mediated energy generation commonly occurs in oceanic surface waters worldwide.
Okada T., et al. The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure. J Mol Biol. 2004, 342(2):571-83. PubMed ID: 15327956

The results suggest that the bond alternation along the unsaturated chain is significant, but weaker in the calculated structure than the one obtained from the X-ray data.
Okada T., et al. Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography. Proc Natl Acad Sci U S A. 2002, 99(9):5982-7. PubMed ID: 11972040

The results show that spectroscopic properties of rhodopsin are similar to those found via bovine rhodopsin in suspension or membrane environment.
Li J., et al. Structure of bovine rhodopsin in a trigonal crystal form. J Mol Biol. 2004, 343(5):1409-38. PubMed ID: 15491621

This article supports a mechanism that involves pivoting movements of kinked helices, which can be coupled to amplified translation of the helix ends near the membrane surfaces while maintaining hydrophobic contacts in the membrane interior.

RHO Preparation Options

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During the past years, Creative Biolabs has successfully generated many functional membrane proteins for our global customers. It’s our responsibility to boost the development of our clients’ programs with our experienced service. For more details, please feel free to contact us.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

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