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Title: Synthetic OCP heterodimers are photoactive and recapitulate the fusion of two primitive carotenoproteins in the evolution of cyanobacterial photoprotection

Journal Article · · The Plant Journal
DOI:https://doi.org/10.1111/tpj.13593· OSTI ID:1596270
 [1];  [2];  [1];  [1];  [3]
  1. Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory
  2. Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
  3. Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory; Univ. of California, Berkeley, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)

Summary The orange carotenoid protein ( OCP ) governs photoprotection in the majority of cyanobacteria. It is structurally and functionally modular, comprised of a C‐terminal regulatory domain ( CTD ), an N‐terminal effector domain ( NTD ) and a ketocarotenoid; the chromophore spans the two domains in the ground state and translocates fully into the NTD upon illumination. Using both the canonical OCP 1 from Fremyella diplosiphon and the presumably more primitive OCP 2 paralog from the same organism, we show that an NTD ‐ CTD heterodimer forms when the domains are expressed as separate polypeptides. The carotenoid is required for the heterodimeric association, assembling an orange complex which is stable in the dark. Both OCP 1 and OCP 2 heterodimers are photoactive, undergoing light‐driven heterodimer dissociation, but differ in their ability to reassociate in darkness, setting the stage for bioengineering photoprotection in cyanobacteria as well as for developing new photoswitches for biotechnology. Additionally, we reveal that homodimeric CTD can bind carotenoid in the absence of NTD , and name this truncated variant the C‐terminal domain‐like carotenoid protein ( CCP ). This finding supports the hypothesis that the OCP evolved from an ancient fusion event between genes for two different carotenoid‐binding proteins ancestral to the NTD and CTD . We suggest that the CCP and its homologs constitute a new family of carotenoproteins within the NTF 2‐like superfamily found across all kingdoms of life.

Research Organization:
Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES); National Science Foundation (NSF)
Grant/Contract Number:
FG02-91ER20021; IOS 1557324; DE‐FG02‐91ER20021
OSTI ID:
1596270
Alternate ID(s):
OSTI ID: 1374081
Journal Information:
The Plant Journal, Vol. 91, Issue 4; ISSN 0960-7412
Publisher:
Society for Experimental BiologyCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 24 works
Citation information provided by
Web of Science

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Cited By (1)

A genetically encoded fluorescent temperature sensor derived from the photoactive Orange Carotenoid Protein journal June 2019

Figures / Tables (5)