Work

Conservation of Molecular Interactions Stabilizing Bovine and Mouse Rhodopsin

Year: 2010

Type: article

Abstract: Rhodopsin is the light receptor that initiates phototransduction in rod photoreceptor cells. The structure and function of rhodopsin are tightly linked to molecular interactions that stabilize and determine the receptor's functional state. Single-molecule force spectroscopy (SMFS) was used to localize and quantify molecular interactions that structurally stabilize bovine and mouse rhodopsin from native disk membranes of rod photoreceptor cells. The mechanical unfolding of bovine and mouse rhodopsin revealed nine major unfolding intermediates, each intermediate defining a structurally stable segment in the receptor. These stable structural segments had similar localization and occurrence in both bovine and mouse samples. For each structural segment, parameters describing their unfolding energy barrier were determined by dynamic SMFS. No major differences were observed between bovine and mouse rhodopsin, thereby implying that the structures of both rhodopsins are largely stabilized by similar molecular interactions.

Source: Biochemistry

DOI: 10.1021/bi101345x

Authors: Shiho Kawamura, Alejandro T. Colozo, Daniel J. Müller, Paul S.-H. Park

Institutions: ETH Zurich, Case Western Reserve University

Language: English

Topic: Force Microscopy Techniques and Applications

Subfield: Atomic and Molecular Physics, and Optics

Field: Physics and Astronomy

Domain: Physical Sciences

Open Access status: green

Funder: National Eye Institute

Awards: G367200232, G4132518751, G89674864