LIGHT-HARVESTING COMPLEXES IN OXYGENIC PHOTOSYNTHESIS: Diversity, Control, and Evolution

Grossman, Arthur R.; Bhaya, Devaki; Apt, Kirk E.; Kehoe, David M.

doi:10.1146/annurev.ge.29.120195.001311

Cited by 266 publications

(137 citation statements)

References 105 publications

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“…The development of molecular tools in the 1970 and 1980s created new opportunities for elucidating the regulation of PBS biosynthesis. By the latter part of the 1980s, most genes encoding PBS structural polypeptides were cloned, sequenced and their expression characterized (summarized in Tandeau de Tandeau de Marsac and Houmard 1993;Grossman et al 1994). Researchers who contributed very significantly to isolating and characterizing genes encoding structural components of the PBS were Don Bryant, Nicole Tandeau de Marsac and members of my own group such as Peggy Lemaux and Pamela Conley.…”

Section: Complementary Chromatic Adaptation From Way Backmentioning

confidence: 99%

“…The vivid pigmentation of cyanobacteria and red algae is mostly a consequence of the presence of the phycobilisome (PBS), an abundant major light harvesting complex that under some conditions can account for 30% of total cellular protein (Tandeau de Marsac and Houmard 1993;Grossman et al 1995). This peripheral membrane complex associates with the outer surface of photosynthetic membranes, absorbing and efficiently transferring excitation energy to the photosynthetic reaction centers Searle et al 1978).…”

Section: Introductionmentioning

confidence: 99%

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A molecular understanding of complementary chromatic adaptation

Grossman

Discoveries in Photosynthesis

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Photosynthetic activity and the composition of the photosynthetic apparatus are strongly regulated by environmental conditions. Some visually dramatic changes in pigmentation of cyanobacterial cells that occur during changing nutrient and light conditions reflect marked alterations in components of the major light-harvesting complex in these organisms, the phycobilisome. As noted well over 100 years ago, the pigment composition of some cyanobacteria is very sensitive to ambient wavelengths of light; this sensitivity reflects molecular changes in polypeptide constituents of the phycobilisome. The levels of different pigmented polypeptides or phycobiliproteins that become associated with the phycobilisome are adjusted to optimize absorption of excitation energy present in the environment. This process, called complementary chromatic adaptation, is controlled by a bilin-binding photoreceptor related to phytochrome of vascular plants; however, many other regulatory elements also play a role in chromatic adaptation. My perspectives and biases on the history and significance of this process are presented in this essay.

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Section: Complementary Chromatic Adaptation From Way Backmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A molecular understanding of complementary chromatic adaptation

Grossman

Discoveries in Photosynthesis

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“…Photosynthetic organisms capture light energy using the light-harvesting antenna system [14]. In higher plants and green algae, the core antenna complexes of the photosystem II (PS II) consist of CP43 and CP47, and those of photosystem I (PSI) consist of P700 chlorophyll b-protein complexes (CP1) [13,14].…”

Section: Introductionmentioning

confidence: 99%

“…In higher plants and green algae, the core antenna complexes of the photosystem II (PS II) consist of CP43 and CP47, and those of photosystem I (PSI) consist of P700 chlorophyll b-protein complexes (CP1) [13,14]. These core antenna complexes contain chlorophyll a and β-carotene as the photosynthetic pigments [4,8].…”

Section: Introductionmentioning

confidence: 99%

Functional analysis of N-terminal domains of Arabidopsis chlorophyllide a oxygenase

Sakuraba

Yamasato

Tanaka

et al. 2007

Plant Physiology and Biochemistry

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Higher plants acclimate to various light environments by changing the antenna size of a light harvesting photosystem. The antenna size of a photosystem is partly determined by the amount of chlorophyll b in the light-harvesting complexes. Chlorophyllide a oxygenase (CAO) converts chlorophyll a to chlorophyll b in a two-step oxygenation reaction. In our previous study, we demonstrated that the cellular level of the CAO protein controls accumulation of chlorophyll b. We found that the amino acids sequences of CAO in higher plants consist of three domains (A, B, and C domains). The C domain exhibits a catalytic function, and we demonstrated that the combination of the A and B domains regulates the cellular level of CAO. However, the individual function of each of A and B domain has not been determined yet. Therefore, in the present study we constructed a series of deleted CAO sequences that were fused with green fluorescent protein and overexpressed in a chlorophyll b-less mutant of Arabidopsis thaliana, ch1-1, to further dissect functions of A and B domains. Subsequent comparative analyses of the transgenic plants overexpressing B-domain containing proteins and those lacking the B domain determined that there was no significant difference in CAO protein levels. These results indicate that the B domain is not involved in the regulation of the CAO protein levels. Taken together, we concluded that the A domain alone is involved in the regulatory mechanism of the CAO protein levels.

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“…Phycobilisomes, the light-harvesting antenna complexes in cyanobacteria and red algae, are supramolecular complexes of phycobiliproteins (PBP) 4 and linkers (1-3); they are packed with hundreds of open-chain tetrapyrrole (bilin) chromophores. These antenna pigments absorb light in the wavelength range between 480 and 660 nm; and their spatial arrangement in the phycobilisome ensures directional energy transfer with high quantum efficiency to the photosynthetic reaction centers (4,5).…”

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confidence: 99%

Structure and Mechanism of the Phycobiliprotein Lyase CpcT

Zhou

Ding

Zeng

et al. 2014

Journal of Biological Chemistry

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Background: Phycobiliprotein lyases catalyze covalent attachment of chromophores to cyanobacterial antenna proteins. Results: We present crystal structures of a T-type lyase and its complex with phycocyanobilin. Conclusion: The proposed reaction mechanism accounts for chromophore stabilization and regio-and stereospecificity. Significance: This work sheds light on a crucial step in phycobiliprotein maturation and provides a model for other types of phycobiliprotein lyases.

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LIGHT-HARVESTING COMPLEXES IN OXYGENIC PHOTOSYNTHESIS: Diversity, Control, and Evolution

Cited by 266 publications

References 105 publications

A molecular understanding of complementary chromatic adaptation

A molecular understanding of complementary chromatic adaptation

Functional analysis of N-terminal domains of Arabidopsis chlorophyllide a oxygenase

Structure and Mechanism of the Phycobiliprotein Lyase CpcT

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