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

Abstract

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 Xray 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.

Authors:
 [1];  [2];  [2];  [3];  [4];  [5];  [5];  [5];  [3];  [3];  [3];  [4];  [1]
  1. Univ. of South Bohemia, České Budějovice (Czech Republic). Inst. of Physics
  2. Michigan State Univ., East Lansing, MI (United States)
  3. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
  4. Michigan State Univ., East Lansing, MI (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
  5. Czech Academy of Sciences, Dolní Břežany (Czech Republic)
Publication Date:
Research Org.:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States); Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
OSTI Identifier:
1581083
Alternate Identifier(s):
OSTI ID: 1575946; OSTI ID: 1734847; OSTI ID: 1735819
Grant/Contract Number:  
AC02-05CH11231; FG02-91ER20021
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Biochimica et Biophysica Acta - Bioenergetics
Additional Journal Information:
Journal Volume: 1861; Journal Issue: 2; Journal ID: ISSN 0005-2728
Publisher:
Elsevier
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; OCP1; OCP2; Photoactivation; X-ray footprinting; Ultrafast spectroscopy

Citation Formats

Kuznetsova, Valentyna, Dominguez-Martin, Maria Agustina, Bao, Han, Gupta, Sayan, Sutter, Markus, Kloz, Miroslav, Rebarz, Mateusz, Přeček, Martin, Chen, Yan, Petzold, Christopher J., Ralston, Corie Y., Kerfeld, Cheryl A., and Polívka, Tomáš. Comparative ultrafast spectroscopy and structural analysis of OCP1 and OCP2 from Tolypothrix. United States: N. p., 2019. Web. doi:10.1016/j.bbabio.2019.148120.
Kuznetsova, Valentyna, Dominguez-Martin, Maria Agustina, Bao, Han, Gupta, Sayan, Sutter, Markus, Kloz, Miroslav, Rebarz, Mateusz, Přeček, Martin, Chen, Yan, Petzold, Christopher J., Ralston, Corie Y., Kerfeld, Cheryl A., & Polívka, Tomáš. Comparative ultrafast spectroscopy and structural analysis of OCP1 and OCP2 from Tolypothrix. United States. https://doi.org/10.1016/j.bbabio.2019.148120
Kuznetsova, Valentyna, Dominguez-Martin, Maria Agustina, Bao, Han, Gupta, Sayan, Sutter, Markus, Kloz, Miroslav, Rebarz, Mateusz, Přeček, Martin, Chen, Yan, Petzold, Christopher J., Ralston, Corie Y., Kerfeld, Cheryl A., and Polívka, Tomáš. Thu . "Comparative ultrafast spectroscopy and structural analysis of OCP1 and OCP2 from Tolypothrix". United States. https://doi.org/10.1016/j.bbabio.2019.148120. https://www.osti.gov/servlets/purl/1581083.
@article{osti_1581083,
title = {Comparative ultrafast spectroscopy and structural analysis of OCP1 and OCP2 from Tolypothrix},
author = {Kuznetsova, Valentyna and Dominguez-Martin, Maria Agustina and Bao, Han and Gupta, Sayan and Sutter, Markus and Kloz, Miroslav and Rebarz, Mateusz and Přeček, Martin and Chen, Yan and Petzold, Christopher J. and Ralston, Corie Y. and Kerfeld, Cheryl A. and Polívka, Tomáš},
abstractNote = {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 Xray 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.},
doi = {10.1016/j.bbabio.2019.148120},
url = {https://www.osti.gov/biblio/1581083}, journal = {Biochimica et Biophysica Acta - Bioenergetics},
issn = {0005-2728},
number = 2,
volume = 1861,
place = {United States},
year = {2019},
month = {11}
}

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