An experimental comparison of human and bovine rhodopsin provides insight into the molecular basis of retinal disease. Issue 12 (31st May 2017)

• Record Type: Journal Article
• Authors: Morrow, James M.; Castiglione, Gianni M.; Dungan, Sarah Z.; Tang, Portia L.; Bhattacharyya, Nihar; Hauser, Frances E.; Chang, Belinda S.W.
• Is Part Of: FEBS letters. Volume 591:Issue 12(2017)
• Page Start: 1720
• Page End: 1731
• Publication Date: 2017-05-31
• Subjects: opsin -- retinal disease -- retinitis pigmentosa -- vision -- visual pigment; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12637
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Rhodopsin is the visual pigment that mediates dim‐light vision in vertebrates and is a model system for the study of retinal disease. The majority of rhodopsin experiments are performed using bovine rhodopsin; however, recent evidence suggests that significant functional differences exist among mammalian rhodopsins. In this study, we identify differences in both thermal decay and light‐activated retinal release rates between bovine and human rhodopsin and perform mutagenesis studies to highlight two clusters of substitutions that contribute to these differences. We also demonstrate that the retinitis pigmentosa‐associated mutation G51A behaves differently in human rhodopsin compared to bovine rhodopsin and determine that the thermal decay rate of an ancestrally reconstructed mammalian rhodopsin displays an intermediate phenotype compared to the two extant pigments. Abstract :