1. Effect of the C-terminal proline repeats on ordered packing of squid rhodopsin and its mobility in membranes
- Author
-
Anthony Davies, Anthony Watts, Catherine Vénien-Bryan, Helen R. Saibil, Keith Langmack, Derek Marsh, and Jenny Baverstock
- Subjects
Rhodopsin ,Hot Temperature ,Proline ,genetic structures ,Biophysics ,Biochemistry ,Spin label ESR (spectroscopy) ,law.invention ,Structural Biology ,law ,Genetics ,Animals ,Electron paramagnetic resonance ,Molecular Biology ,Repetitive Sequences, Nucleic Acid ,biology ,Chemistry ,Cell Membrane ,2D crystal ,Decapodiformes ,Electron Spin Resonance Spectroscopy ,Cell Biology ,Negative stain ,Peptide Fragments ,Rotational diffusion ,Cephalopod rhodopsin ,Microscopy, Electron ,Crystallography ,Membrane ,Membrane protein ,biology.protein ,Nucleic acid ,Photoreceptor Cells, Invertebrate ,sense organs ,Electron microscope ,Negative stain electron microscopy - Abstract
Negative stain electron microscopy and saturation transfer electron spin resonance spectroscopy have been used to compare the lattice ordering and in-plane membrane mobility of full-length and C-terminally cleaved squid rhodopsin. The C-terminus of squid rhodopsin contains a negatively charged region followed by 9–10 repeats of a proline-rich sequence, not found in rhodopsins other than those of cephalopod invertebrates, but similar proline repeats are found in other, unrelated membrane proteins. We find that the proline repeats cluster the rhodopsins into small groups, interfering with two-dimensional crystallization and maintaining their mobility in the membrane.
- Published
- 2016
- Full Text
- View/download PDF