Comparative ultrafast spectroscopy and structural analysis of OCP1 and OCP2 from Tolypothrix

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F20%3A43901336" target="_blank" >RIV/60076658:12310/20:43901336 - isvavai.cz</a>

Alternative codes found

RIV/68378271:_____/20:00537885

Result on the web

<a href="https://www.sciencedirect.com/science/article/pii/S0005272819301690?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0005272819301690?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bbabio.2019.148120" target="_blank" >10.1016/j.bbabio.2019.148120</a>

Result language

angličtina

Original language name

Comparative ultrafast spectroscopy and structural analysis of OCP1 and OCP2 from Tolypothrix

Original language description

The orange carotenoid protein (OCP) is a structurally and functionally modular photoactive protein involved in cyanobacterial photoprotection. Recently, based on bioinformatic analysis and phylogenetic relationships, new families of OCP have been described, OCP2 and OCPx. The first characterization of the OCP2 showed both faster photoconversion and back-conversion, and lower fluorescence quenching of phycobilisomes relative to the well-characterized OCP1. Moreover, OCP2 is not regulated by the fluorescence recovery protein (FRP). In this work, we present a comprehensive study combining ultrafast spectroscopy and structural analysis to compare the photoactivation mechanisms of OCP1 and OCP2 from Tolypothrix PCC 7601. We show that despite significant differences in their functional characteristics, the spectroscopic properties of OCP1 and OCP2 are comparable. This indicates that the OCP functionality is not directly related to the spectroscopic properties of the bound carotenoid. In addition, the structural analysis by X-ray footprinting reveals that, overall, OCP1 and OCP2 have grossly the same photoactivation mechanism. However, the OCP2 is less reactive to radiolytic labeling, suggesting that the protein is less flexible than OCP1. This observation could explain fast photoconversion of OCP2.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10610 - Biophysics

Project

<a href="/en/project/GA18-21631S" target="_blank" >GA18-21631S: Ultrafast spectroscopy as a tool for elucidation the structure-function relationship in cyanobacterial carotenoid-binding proteins</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2020

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Biochimica et Biophysica Acta - Bioenergetics

ISSN

0005-2728

e-ISSN

—

Volume of the periodical

1861

Issue of the periodical within the volume

2

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

11

Pages from-to

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UT code for WoS article

000508749700003

EID of the result in the Scopus database

2-s2.0-85075539802