Oligomerization state and pigment binding strength of the peridinin-Chl a-protein

Jing Jiang; Hao Zhang; Xun Lu; Yue Lu; Matthew J. Cuneo; Hugh M. O'Neill; Volker Urban; Cynthia S. Lo; Robert E. Blankenship

doi:10.1016/j.febslet.2015.07.039

Oligomerization state and pigment binding strength of the peridinin-Chl a-protein

Jing Jiang, Hao Zhang, Xun Lu, Yue Lu, Matthew J. Cuneo, Hugh M. O'Neill, Volker Urban, Cynthia S. Lo, Robert E. Blankenship

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

The peridinin-chlorophyll a-protein (PCP) is one of the major light harvesting complexes (LHCs) in photosynthetic dinoflagellates. We analyzed the oligomeric state of PCP isolated from the dinoflagellate Symbiodinium, which has received increasing attention in recent years because of its role in coral bleaching. Size-exclusion chromatography (SEC) and small angle neutron scattering (SANS) analysis indicated PCP exists as monomers. Native mass spectrometry (native MS) demonstrated two oligomeric states of PCP, with the monomeric PCP being dominant. The trimerization may not be necessary for PCP to function as a light-harvesting complex.

Original language	English
Pages (from-to)	2713-2719
Number of pages	7
Journal	FEBS Letters
Volume	589
Issue number	19
DOIs	https://doi.org/10.1016/j.febslet.2015.07.039
State	Published - Sep 14 2015

Funding

The authors would like to thank Drs. David Kramer and Atsuko Kanazawa of Michigan State University for providing the Symbiodinium culture, and Ms. Mindy Prado for helping with cell culturing. This research is from the Photosynthetic Antenna Research Center (PARC), an Energy Frontier Research Center funded by the DOE, Office of Science, Office of Basic Energy Sciences under Award Number DE-SC 0001035 . The Center for Structural Molecular Biology operates Bio-SANS and is supported by the U.S. DOE, Office of Science, Office of Biological and Environmental Research under FWP ERKP291 . The High Flux Isotope Reactor is sponsored by the Scientific User Facilities Division, Basic Energy Sciences . Oak Ridge National Laboratory (ORNL) is managed by UT-Battelle, LLC, for the U. S. Department of Energy (DOE) under contract No. DE-AC05-00OR22725.

Funders	Funder number
Photosynthetic Antenna Research Center
U.S. Department of Energy	DE-AC05-00OR22725
Office of Science
Basic Energy Sciences	DE-SC 0001035
Biological and Environmental Research	FWP ERKP291
Oak Ridge National Laboratory

Keywords

Chlorophyll
Dinoflagellate
Light-harvesting
Native mass spectrometry
Peridinin
Photosynthesis
Symbiodinium

Access to Document

10.1016/j.febslet.2015.07.039

Cite this

@article{b5b881624fef403b9b4e9208bb601f98,

title = "Oligomerization state and pigment binding strength of the peridinin-Chl a-protein",

abstract = "The peridinin-chlorophyll a-protein (PCP) is one of the major light harvesting complexes (LHCs) in photosynthetic dinoflagellates. We analyzed the oligomeric state of PCP isolated from the dinoflagellate Symbiodinium, which has received increasing attention in recent years because of its role in coral bleaching. Size-exclusion chromatography (SEC) and small angle neutron scattering (SANS) analysis indicated PCP exists as monomers. Native mass spectrometry (native MS) demonstrated two oligomeric states of PCP, with the monomeric PCP being dominant. The trimerization may not be necessary for PCP to function as a light-harvesting complex.",

keywords = "Chlorophyll, Dinoflagellate, Light-harvesting, Native mass spectrometry, Peridinin, Photosynthesis, Symbiodinium",

author = "Jing Jiang and Hao Zhang and Xun Lu and Yue Lu and Cuneo, {Matthew J.} and O'Neill, {Hugh M.} and Volker Urban and Lo, {Cynthia S.} and Blankenship, {Robert E.}",

year = "2015",

month = sep,

day = "14",

doi = "10.1016/j.febslet.2015.07.039",

language = "English",

volume = "589",

pages = "2713--2719",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "wiley",

number = "19",

}

TY - JOUR

T1 - Oligomerization state and pigment binding strength of the peridinin-Chl a-protein

AU - Jiang, Jing

AU - Zhang, Hao

AU - Lu, Xun

AU - Lu, Yue

AU - Cuneo, Matthew J.

AU - O'Neill, Hugh M.

AU - Urban, Volker

AU - Lo, Cynthia S.

AU - Blankenship, Robert E.

PY - 2015/9/14

Y1 - 2015/9/14

N2 - The peridinin-chlorophyll a-protein (PCP) is one of the major light harvesting complexes (LHCs) in photosynthetic dinoflagellates. We analyzed the oligomeric state of PCP isolated from the dinoflagellate Symbiodinium, which has received increasing attention in recent years because of its role in coral bleaching. Size-exclusion chromatography (SEC) and small angle neutron scattering (SANS) analysis indicated PCP exists as monomers. Native mass spectrometry (native MS) demonstrated two oligomeric states of PCP, with the monomeric PCP being dominant. The trimerization may not be necessary for PCP to function as a light-harvesting complex.

AB - The peridinin-chlorophyll a-protein (PCP) is one of the major light harvesting complexes (LHCs) in photosynthetic dinoflagellates. We analyzed the oligomeric state of PCP isolated from the dinoflagellate Symbiodinium, which has received increasing attention in recent years because of its role in coral bleaching. Size-exclusion chromatography (SEC) and small angle neutron scattering (SANS) analysis indicated PCP exists as monomers. Native mass spectrometry (native MS) demonstrated two oligomeric states of PCP, with the monomeric PCP being dominant. The trimerization may not be necessary for PCP to function as a light-harvesting complex.

KW - Chlorophyll

KW - Dinoflagellate

KW - Light-harvesting

KW - Native mass spectrometry

KW - Peridinin

KW - Photosynthesis

KW - Symbiodinium

UR - http://www.scopus.com/inward/record.url?scp=84941426406&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2015.07.039

DO - 10.1016/j.febslet.2015.07.039

M3 - Article

C2 - 26241331

AN - SCOPUS:84941426406

SN - 0014-5793

VL - 589

SP - 2713

EP - 2719

JO - FEBS Letters

JF - FEBS Letters

IS - 19

ER -

Oligomerization state and pigment binding strength of the peridinin-Chl a-protein

Abstract

Funding

Keywords

Access to Document

Other files and links

Fingerprint

Cite this