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Light-induced structural adaptation of the bundle-shaped phycobilisome from thylakoid-lacking cyanobacterium Gloeobacter violaceus
by
Sun, Shan
, Ma, Jianfei
, You, Xin
, Sui, Sen-Fang
in
101/28
/ 631/449/1734/2077
/ 631/535/1258/1259
/ Adaptation
/ Adaptation, Physiological
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Carotenoids
/ Cryoelectron Microscopy
/ Cyanobacteria
/ Cyanobacteria - metabolism
/ Cyanobacteria - radiation effects
/ Cyanobacteria - ultrastructure
/ Energy transfer
/ Humanities and Social Sciences
/ Light
/ Light effects
/ Light intensity
/ Luminous intensity
/ Membranes
/ Microscopy
/ multidisciplinary
/ Phycobilisomes
/ Phycobilisomes - chemistry
/ Phycobilisomes - metabolism
/ Phycobilisomes - radiation effects
/ Phycobilisomes - ultrastructure
/ Phylogenetics
/ Proteins
/ Science
/ Science (multidisciplinary)
/ Structural members
/ Thylakoid membranes
/ Thylakoids - metabolism
/ Thylakoids - radiation effects
/ Thylakoids - ultrastructure
2025
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Light-induced structural adaptation of the bundle-shaped phycobilisome from thylakoid-lacking cyanobacterium Gloeobacter violaceus
by
Sun, Shan
, Ma, Jianfei
, You, Xin
, Sui, Sen-Fang
in
101/28
/ 631/449/1734/2077
/ 631/535/1258/1259
/ Adaptation
/ Adaptation, Physiological
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Carotenoids
/ Cryoelectron Microscopy
/ Cyanobacteria
/ Cyanobacteria - metabolism
/ Cyanobacteria - radiation effects
/ Cyanobacteria - ultrastructure
/ Energy transfer
/ Humanities and Social Sciences
/ Light
/ Light effects
/ Light intensity
/ Luminous intensity
/ Membranes
/ Microscopy
/ multidisciplinary
/ Phycobilisomes
/ Phycobilisomes - chemistry
/ Phycobilisomes - metabolism
/ Phycobilisomes - radiation effects
/ Phycobilisomes - ultrastructure
/ Phylogenetics
/ Proteins
/ Science
/ Science (multidisciplinary)
/ Structural members
/ Thylakoid membranes
/ Thylakoids - metabolism
/ Thylakoids - radiation effects
/ Thylakoids - ultrastructure
2025
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Light-induced structural adaptation of the bundle-shaped phycobilisome from thylakoid-lacking cyanobacterium Gloeobacter violaceus
by
Sun, Shan
, Ma, Jianfei
, You, Xin
, Sui, Sen-Fang
in
101/28
/ 631/449/1734/2077
/ 631/535/1258/1259
/ Adaptation
/ Adaptation, Physiological
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Carotenoids
/ Cryoelectron Microscopy
/ Cyanobacteria
/ Cyanobacteria - metabolism
/ Cyanobacteria - radiation effects
/ Cyanobacteria - ultrastructure
/ Energy transfer
/ Humanities and Social Sciences
/ Light
/ Light effects
/ Light intensity
/ Luminous intensity
/ Membranes
/ Microscopy
/ multidisciplinary
/ Phycobilisomes
/ Phycobilisomes - chemistry
/ Phycobilisomes - metabolism
/ Phycobilisomes - radiation effects
/ Phycobilisomes - ultrastructure
/ Phylogenetics
/ Proteins
/ Science
/ Science (multidisciplinary)
/ Structural members
/ Thylakoid membranes
/ Thylakoids - metabolism
/ Thylakoids - radiation effects
/ Thylakoids - ultrastructure
2025
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Light-induced structural adaptation of the bundle-shaped phycobilisome from thylakoid-lacking cyanobacterium Gloeobacter violaceus
Journal Article
Light-induced structural adaptation of the bundle-shaped phycobilisome from thylakoid-lacking cyanobacterium Gloeobacter violaceus
2025
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Overview
Gloeobacter
diverged from other lineages early in cyanobacterial evolution, preferentially growing under low light intensity conditions. Among cyanobacteria,
G. violaceus
exhibits unique features, including lack of a thylakoid membrane and bundle-shaped antenna phycobilisomes (PBSs), densely packed and well-organized on the plasma membrane. However, without high-resolution structures, it has remained unclear how
G. violaceus
PBSs assemble into a bundle-shaped configuration. Here we solve the cryo-EM structures of PBSs from
G. violaceus
cells cultured under low (Sr-PBS) or moderate (Lr-PBS) light intensity. These structures reveal two unique linker proteins, L
RC
91kDa
and L
RC
81kDa
, that play a key role in the PBS architecture. Analysis of the bilin arrangement indicates that the bundle-shaped structure allows efficient energy transfer among rods. Moreover, comparison between Lr-PBS and Sr-PBS uncovers a distinct mode of adaption to increased light intensity wherein the ApcA
2
-ApcB
3
-ApcD layer can be blocked from binding to the core by altering structural elements exclusively found in the
G. violaceus
L
CM
. This study illustrates previously unrecognized mechanisms of assembly and adaptation to varying light intensity in the bundle-shaped PBS of
G. violaceus
.
Gloeobacter
diverged from other lineages early in cyanobacterial evolution, preferentially growing under low light intensity conditions. Here, the authors describe cryo-EM structures of PBSs from
G. violaceus
cells cultured under low or moderate light intensity.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Cyanobacteria - radiation effects
/ Cyanobacteria - ultrastructure
/ Humanities and Social Sciences
/ Light
/ Phycobilisomes - radiation effects
/ Phycobilisomes - ultrastructure
/ Proteins
/ Science
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