Proteomics

Dataset Information

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Retinal-cysteine adduct in Opn5L1


ABSTRACT: Targeted analysis of retinal-cysteine adduct in Opsin 5 like-1 (Opn5L1) protein Chicken Opn5L1 E177K/Q192K mutant was expressed in HEK293T, regenerated by all-trans-retinal, solubilized by dodecyl maltoside, and purified using Rho1D4 antibody-conjugated Sephalose. Semi-quantitative targeted analyses of trypsinized Opn5L1 with or without light irradiation were carried out using reverse phase LC-ESI-MSn to detect light-dependent formation of retinal-cysteine adduct. The results were analyzed by Mass++, mMass and Igor Pro softwares.

ORGANISM(S): Gallus Gallus

SUBMITTER: Yoshinori Shichida 

PROVIDER: PXD008890 | JPOST Repository | Thu Feb 15 00:00:00 GMT 2018

REPOSITORIES: jPOST

Dataset's files

Source:
Action DRS
Dark.RAW Raw
Dark_MS2_mMass%20Report.html Other
Dark_MS2_mMass_spectrum.png Other
Dark_MS2_peaklist.mgf Mgf
Dark_MS2_spectrum.txt Txt
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Publications


Most opsins are G protein-coupled receptors that utilize retinal both as a ligand and as a chromophore. Opsins' main established mechanism is light-triggered activation through retinal 11-cis-to-all-trans photoisomerization. Here we report a vertebrate non-visual opsin that functions as a Gi-coupled retinal receptor that is deactivated by light and can thermally self-regenerate. This opsin, Opn5L1, binds exclusively to all-trans-retinal. More interestingly, the light-induced deactivation through  ...[more]

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