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 journalArticlepeer-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 languageEnglish
Pages (from-to)2713-2719
Number of pages7
JournalFEBS Letters
Volume589
Issue number19
DOIs
StatePublished - Sep 14 2015

Bibliographical note

Publisher Copyright:
© 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Keywords

  • Chlorophyll
  • Dinoflagellate
  • Light-harvesting
  • Native mass spectrometry
  • Peridinin
  • Photosynthesis
  • Symbiodinium

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