skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Light regulation of pigment and photosystem biosynthesis in cyanobacteria

; ; ; ;
Publication Date:
Research Org.:
Energy Frontier Research Centers (EFRC) (United States). Photosynthetic Antenna Research Center (PARC)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
DOE Contract Number:
Resource Type:
Journal Article
Resource Relation:
Journal Name: Current Opinion in Plant Biology; Journal Volume: 37; Journal Issue: C; Related Information: PARC partners with Washington University in St. Louis (lead); University of California, Riverside; University of Glasgow, UK; Los Alamos National Laboratory; University of New Mexico; New Mexico Corsortium; North Carolina State University; Northwestern University; Oak Ridge National Laboratory; University of Pennsylvania; Sandia National Laboratories; University of Sheffield, UK
Country of Publication:
United States
solar (fuels), photosynthesis (natural and artificial), biofuels (including algae and biomass), bio-inspired, charge transport, membrane, synthesis (novel materials), synthesis (self-assembly)

Citation Formats

Ho, Ming-Yang, Soulier, Nathan T., Canniffe, Daniel P., Shen, Gaozhong, and Bryant, Donald A. Light regulation of pigment and photosystem biosynthesis in cyanobacteria. United States: N. p., 2017. Web. doi:10.1016/j.pbi.2017.03.006.
Ho, Ming-Yang, Soulier, Nathan T., Canniffe, Daniel P., Shen, Gaozhong, & Bryant, Donald A. Light regulation of pigment and photosystem biosynthesis in cyanobacteria. United States. doi:10.1016/j.pbi.2017.03.006.
Ho, Ming-Yang, Soulier, Nathan T., Canniffe, Daniel P., Shen, Gaozhong, and Bryant, Donald A. Thu . "Light regulation of pigment and photosystem biosynthesis in cyanobacteria". United States. doi:10.1016/j.pbi.2017.03.006.
title = {Light regulation of pigment and photosystem biosynthesis in cyanobacteria},
author = {Ho, Ming-Yang and Soulier, Nathan T. and Canniffe, Daniel P. and Shen, Gaozhong and Bryant, Donald A.},
abstractNote = {},
doi = {10.1016/j.pbi.2017.03.006},
journal = {Current Opinion in Plant Biology},
number = C,
volume = 37,
place = {United States},
year = {Thu Jun 01 00:00:00 EDT 2017},
month = {Thu Jun 01 00:00:00 EDT 2017}
  • Cited by 5
  • The light-harvesting complex of photosystem I (LHCI) was isolated from wild-type cells of Chlamydomonas reinhardtii; the Chl a/b-protein complex contains four major polypeptides of approximately 27, 26, 24, and 20 kDa (polypeptides 14, 15, 17.2, and 22, respectively, in the nomenclature for Chlamydomonas thylakoid proteins). Antiserum against the 20-kDa subunit of LHCI was prepared and used to determine the membrane topology, subcellular site of synthesis, and cell-cycle regulation of this polypeptide. The results indicate that the 20-kDa subunit as well as the other major LHCI polypeptides are integral membrane proteins. Moreover, protease digestion experiments reveal that the 20-kDa polypeptide ismore » completely protected by the membrane bilayer but the 27- and 26-kDa LHCI polypeptides are exposed at the membrane surface. In vivo synthesis of the 20-kDa polypeptide is sensitive to cycloheximide but not to chloramphenicol; the form of the polypeptide recovered from in vitro translations of polyadenylated RNA is approximately 24 kDa, 4 kDa larger than the mature polypeptide. It is concluded that this LHCI polypeptide is nuclear encoded and synthesized in the cytoplasm as a higher molecular weight precursor. Synthesis of the 20-kDa polypeptide is restricted to the light period in light-dark synchronized cells. Translatable mRNA for this polypeptide accumulates during the light but levels are dramatically reduced during the dark period. Thus, synthesis of the 20-kDa subunit of LHCI appears to be transcriptionally regulated during the cell cycle.« less
  • The photosystem II (PSII) protein PsbS and the enzyme violaxanthin deepoxidase (VDE) are known to influence the dynamics of energy-dependent quenching (qE), the component of nonphotochemical quenching (NPQ) that allows plants to respond to fast fluctuations in light intensity. Although the absence of PsbS and VDE has been shown to change the amount of quenching, there have not been any measurements that can detect whether the presence of these proteins alters the type of quenching that occurs. The chlorophyll fluorescence lifetime probes the excited-state chlorophyll relaxation dynamics and can be used to determine the amount of quenching as well asmore » whether two different genotypes with the same amount of NPQ have similar dynamics of excited-state chlorophyll relaxation. We measured the fluorescence lifetimes on whole leaves of Arabidopsis thaliana throughout the induction and relaxation of NPQ for wild type and the qE mutants, npq4, which lacks PsbS; npq1, which lacks VDE and cannot convert violaxanthin to zeaxanthin; and npq1 npq4, which lacks both VDE and PsbS. These measurements show that although PsbS changes the amount of quenching and the rate at which quenching turns on, it does not affect the relaxation dynamics of excited chlorophyll during quenching. In addition, the data suggest that PsbS responds not only to ΔpH but also to the Δψ across the thylakoid membrane. In contrast, the presence of VDE, which is necessary for the accumulation of zeaxanthin, affects the excited-state chlorophyll relaxation dynamics.« less