Ecological diversification of a cyanobacterium through divergence of its novel chlorophyll d-based light-harvesting system

Ulrich, Nikea J.; Shen, Gaozhong; Bryant, Donald A.; Miller, Scott R.

doi:10.1016/j.cub.2024.05.022

Current Biology

2024

DOI: 10.1016/j.cub.2024.05.022

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Ecological diversification of a cyanobacterium through divergence of its novel chlorophyll d-based light-harvesting system

Nikea J. Ulrich,

Gaozhong Shen,

Donald A. Bryant

et al.

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2024

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Cited by 4 publications

References 63 publications

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Presence of low-energy chlorophylls d in photosystem I trimer and monomer cores isolated from Acaryochloris sp. NBRC 102871

Nagao,

Yamamoto,

Ogawa

et al. 2024

Photosynth Res

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Presence of low-energy chlorophylls d in photosystem I trimer and monomer cores isolated from Acaryochloris sp. NBRC 102871

Nagao,

Yamamoto,

Ogawa

et al. 2024

Photosynth Res

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Evolution: Spectral speciation

Swingley

2024

Current Biology

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The structural basis for light harvesting in organisms producing phycobiliproteins

Bryant,

Gisriel

2024

The Plant Cell

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Cyanobacteria, red algae, and cryptophytes produce two classes of proteins for light-harvesting: water-soluble phycobiliproteins and membrane-intrinsic proteins that bind chlorophylls and carotenoids. In cyanobacteria, red algae, and glaucophytes, phycobilisomes (PBS) are complexes of brightly colored phycobiliproteins and linker (assembly) proteins. To date, six structural classes of phycobilisomes have been described: hemiellipsoidal, block-shaped, hemidiscoidal, bundle-shaped, paddle-shaped, and far-red-light bicylindrical. Two additional antenna complexes containing single types of phycobiliproteins have also been described. Since 2017, structures have been reported for examples of all of these complexes except bundle-shaped phycobilisomes by cryogenic electron microscopy. Phycobilisomes range in size from about 4.6 to 18 MDa and can include ∼900 polypeptides and bind >2000 chromophores. Cyanobacteria additionally produce membrane-associated proteins of the PsbC/CP43 superfamily of Chl a/b/d-binding proteins, including the iron-stress protein IsiA and other paralogous chlorophyll-binding proteins that can form antenna complexes with Photosystem I and/or Photosystem II. Red and cryptophyte algae also produce chlorophyll-binding proteins associated with Photosystem I but which belong to the chlorophyll a/b-binding (CAB) protein superfamily and which are unrelated to the chlorophyll-binding proteins (CBP) of cyanobacteria. This review describes recent progress in structure determination for phycobilisomes and the chlorophyll proteins of cyanobacteria, red algae, and cryptophytan algae.

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Ecological diversification of a cyanobacterium through divergence of its novel chlorophyll d-based light-harvesting system

Cited by 4 publications

References 63 publications

Presence of low-energy chlorophylls d in photosystem I trimer and monomer cores isolated from Acaryochloris sp. NBRC 102871

Presence of low-energy chlorophylls d in photosystem I trimer and monomer cores isolated from Acaryochloris sp. NBRC 102871

Evolution: Spectral speciation

The structural basis for light harvesting in organisms producing phycobiliproteins

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