Oct 30, 2018

Neutralization of a Distributed Coulombic Switch Precisely Tunes Reflectin Assembly

BioRxiv : the Preprint Server for Biology
Robert LevensonDaniel E Morse

Abstract

Reflectin proteins are widely distributed in reflective structures in cephalopods, but only in Loliginid squids are they and the sub-wavelength photonic structures they control dynamically tunable, driving changes in skin color for camouflage and communication. The reflectins are block copolymers with repeated canonical domains interspersed with cationic linkers. Neurotransmitter-activated signal transduction culminates in catalytic phosphorylation of the tunable reflectins' cationic linkers, with the resulting charge-neutralization overcoming Coulombic repulsion to progressively allow condensation and concommitant assembly to form multimeric spheres of tunable size. Structural transitions of reflectins A1 and A2 were analyzed by dynamic light scattering, transmission electron microscopy, solution small angle x-ray scattering, circular dichroism, atomic force microscopy, and fluorimetry. We analyzed the assembly behavior of phospho-mimetic, deletion, and other mutants in conjunction with pH-titration as an in vitro surrogate of phosphorylation to discover a predictive relationship between the extent of neutralization of the protein's net charge density and the size of resulting multimeric protein assemblies of narrow polydisper...Continue Reading

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Mentioned in this Paper

Squid
Base
Size
Fluorometry
Valyl-seryl-tryptophyl-phenylalanyl-phenylalanyl-glutamic acid
Small Angle X Ray Scattering
PHOSPHO1
Plain X-ray
IgA1
Protein Phosphorylation

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