Arrestin-1 engineering facilitates complex stabilization with native rhodopsin.

ABSTRACT: Arrestin-1 desensitizes the activated and phosphorylated photoreceptor rhodopsin by forming transient rhodopsin-arrestin-1 complexes that eventually decay to opsin, retinal and arrestin-1. Via a multi-dimensional screening setup, we identified and combined arrestin-1 mutants that form lasting complexes with light-activated and phosphorylated rhodopsin in harsh conditions, such as high ionic salt concentration. Two quadruple mutants, D303A + T304A + E341A + F375A and R171A + T304A + E341A + F375A share similar heterologous expression and thermo-stability levels with wild type (WT) arrestin-1, but are able to stabilize complexes with rhodopsin with more than seven times higher half-maximal inhibitory concentration (IC₅₀) values for NaCl compared to the WT arrestin-1 protein. These

SUBMITTER: Haider RS 

PROVIDER: S-EPMC6346018 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature