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PLoS One
2015 Oct 20;1010:e0141114. doi: 10.1371/journal.pone.0141114.
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Rhodopsin Forms Nanodomains in Rod Outer Segment Disc Membranes of the Cold-Blooded Xenopus laevis.
Rakshit T
,
Senapati S
,
Sinha S
,
Whited AM
,
Park PS
.
???displayArticle.abstract??? Rhodopsin forms nanoscale domains (i.e., nanodomains) in rod outer segment disc membranes from mammalian species. It is unclear whether rhodopsin arranges in a similar manner in amphibian species, which are often used as a model system to investigate the function of rhodopsin and the structure of photoreceptor cells. Moreover, since samples are routinely prepared at low temperatures, it is unclear whether lipid phase separation effects in the membrane promote the observed nanodomain organization of rhodopsin from mammalian species. Rod outer segment disc membranes prepared from the cold-blooded frog Xenopus laevis were investigated by atomic force microscopy to visualize the organization of rhodopsin in the absence of lipid phase separation effects. Atomic force microscopy revealed that rhodopsin nanodomains form similarly as that observed previously in mammalian membranes. Formation of nanodomains in ROS disc membranes is independent of lipid phase separation and conserved among vertebrates.
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Fig 1. AFM image of an intact murine ROS disc. (A, B) Height (A) and deflection (B) images obtained by contact mode AFM generated using low force. (C, D) Height (C) and deflection (D) images obtained by contact mode AFM generated using higher force. The rim region (1) and nanodomains in the lamellar region (2) are discernible. Height images were scaled to a height range of 38 nm. Scale bar, 250 nm. Illustrations of a disc adsorbed on mica scanned by the AFM tip at low and high forces are shown next to AFM images. (E) A height profile is shown for the cross-section highlighted by a dotted line in panel C.
Fig 2. Murine ROS disc membranes imaged at 37°C. Representative images obtained by tapping mode AFM are shown. Murine ROS disc membranes were prepared at 4°C and imaged at 37°C. Height (left) and amplitude (right) images are shown. Height images were scaled to a height range of 25 nm. Scale bar, 500 nm.
Fig 3. X. laevis ROS disc membrane preparation. (A) The secondary structure of rhodopsin is shown with amino acid residue differences in X. laevis (red) and murine (blue) rhodopsin highlighted. (B) Light microscopy image of purified ROS from the retina of X. laevis. Scale bar, 15 μm. (C) SDS-PAGE of X. laevis (lane 1) and murine (lane 2) ROS disc membrane preparations. The sizes of protein standards are indicated in kDa.
Fig 4. AFM images of X. laevis ROS disc membranes. (A-G) Representative deflection images of X. laevis ROS disc membranes obtained by contact mode AFM. ROS disc membranes exhibit a varying number of lobes, which are formed by deeply penetrating incisures. Scale bar, 500 nm. (H) Histogram of nanodomain sizes measured in 57 images of X. laevis ROS disc membranes. The data was fit by a Log Gaussian function (n = 14,390).
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