TY - JOUR
T1 - Efficient light harvesting in a dark, hot, acidic environment
T2 - The structure and function of PSI-LHCI from Galdieria sulphuraria
AU - Thangaraj, Balakumar
AU - Jolley, Craig C.
AU - Sarrou, Iosifina
AU - Bultema, Jelle B.
AU - Greyslak, Jason
AU - Whitelegge, Julian P.
AU - Lin, Su
AU - Kouřil, Roman
AU - Subramanyam, Rajagopal
AU - Boekema, Egbert J.
AU - Fromme, Petra
N1 - Funding Information:
This work was supported by a grant from the National Science Foundation (0417142 to P.F.).
PY - 2011/1/5
Y1 - 2011/1/5
N2 - Photosystem I-light harvesting complex I (PSI-LHCI) was isolated from the thermoacidophilic red alga Galdieria sulphuraria, and its structure, composition, and light-harvesting function were characterized by electron microscopy, mass spectrometry, and ultrafast optical spectroscopy. The results show that Galdieria PSI is a monomer with core features similar to those of PSI from green algae, but with significant differences in shape and size. A comparison with the crystal structure of higher plant (pea) PSI-LHCI indicates that Galdieria PSI binds seven to nine light-harvesting proteins. Results from ultrafast optical spectroscopy show that the functional coupling of the LHCI proteins to the PSI core is tighter than in other eukaryotic PSI-LHCI systems reported thus far. This tight coupling helps Galdieria perform efficient light harvesting under the low-light conditions present in its natural endolithic habitat.
AB - Photosystem I-light harvesting complex I (PSI-LHCI) was isolated from the thermoacidophilic red alga Galdieria sulphuraria, and its structure, composition, and light-harvesting function were characterized by electron microscopy, mass spectrometry, and ultrafast optical spectroscopy. The results show that Galdieria PSI is a monomer with core features similar to those of PSI from green algae, but with significant differences in shape and size. A comparison with the crystal structure of higher plant (pea) PSI-LHCI indicates that Galdieria PSI binds seven to nine light-harvesting proteins. Results from ultrafast optical spectroscopy show that the functional coupling of the LHCI proteins to the PSI core is tighter than in other eukaryotic PSI-LHCI systems reported thus far. This tight coupling helps Galdieria perform efficient light harvesting under the low-light conditions present in its natural endolithic habitat.
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U2 - 10.1016/j.bpj.2010.09.069
DO - 10.1016/j.bpj.2010.09.069
M3 - Article
C2 - 21190665
AN - SCOPUS:78651236470
VL - 100
SP - 135
EP - 143
JO - Biophysical Journal
JF - Biophysical Journal
SN - 0006-3495
IS - 1
ER -