TY - JOUR
T1 - Thylakoid membrane lipid sulfoquinovosyl-diacylglycerol (SQDG) is required for full functioning of photosystem II in Thermosynechococcus elongatus
AU - Nakajima, Yoshiki
AU - Umena, Yasufumi
AU - Nagao, Ryo
AU - Endo, Kaichiro
AU - Kobayashi, Koichi
AU - Akita, Fusamichi
AU - Suga, Michihiro
AU - Wada, Hajime
AU - Noguchi, Takumi
AU - Shen, Jian Ren
N1 - Funding Information:
This work was supported by Japan Society for the Promotion of Science KAKENHI Grants JP17H06434 (to J.-R. S.), JP16K21181 (to F. A.), and JP15H05588 and JP16KT0058 (to Y. U.), and PRESTO from Japan Science and Technology Agency Grant JPMJPR16P1 of MEXT, Japan (to F. A.). The authors declare that they have no conflicts of interest with the contents of this article. We thank the staff members at beamlines BL41XU and BL38B1 of SPring-8 for their help in data collection under the proposal numbers 2016A2542, 2016B2542, 2017A2535, 2017B2535, 2017A2529, 2017B2529, and 2017B6704.
Publisher Copyright:
© 2018 Nakajima et al.
PY - 2018/9/21
Y1 - 2018/9/21
N2 - Sulfoquinovosyl-diacylglycerol (SQDG) is one of the four lipids present in the thylakoid membranes. Depletion of SQDG causes different degrees of effects on photosynthetic growth and activities in different organisms. Four SQDG molecules bind to each monomer of photosystem II (PSII), but their role in PSII function has not been characterized in detail, and no PSII structure without SQDG has been reported. We analyzed the activities of PSII from an SQDG-deficient mutant of the cyanobacterium Thermosynechococcus elongatus by various spectroscopic methods, which showed that depletion of SQDG partially impaired the PSII activity by impairing secondary quinone (QB) exchange at the acceptor site. We further solved the crystal structure of the PSII dimer from the SQDG deletion mutant at 2.1 Å resolution and found that all of the four SQDG-binding sites were occupied by other lipids, most likely PG molecules. Replacement of SQDG at a site near the head of QB provides a possible explanation for the QB impairment. The replacement of two SQDGs located at the monomer–monomer interface by other lipids decreased the stability of the PSII dimer, resulting in an increase in the amount of PSII monomer in the mutant. The present results thus suggest that although SQDG binding in all of the PSII-binding sites is necessary to fully maintain the activity and stability of PSII, replacement of SQDG by other lipids can partially compensate for their functions.
AB - Sulfoquinovosyl-diacylglycerol (SQDG) is one of the four lipids present in the thylakoid membranes. Depletion of SQDG causes different degrees of effects on photosynthetic growth and activities in different organisms. Four SQDG molecules bind to each monomer of photosystem II (PSII), but their role in PSII function has not been characterized in detail, and no PSII structure without SQDG has been reported. We analyzed the activities of PSII from an SQDG-deficient mutant of the cyanobacterium Thermosynechococcus elongatus by various spectroscopic methods, which showed that depletion of SQDG partially impaired the PSII activity by impairing secondary quinone (QB) exchange at the acceptor site. We further solved the crystal structure of the PSII dimer from the SQDG deletion mutant at 2.1 Å resolution and found that all of the four SQDG-binding sites were occupied by other lipids, most likely PG molecules. Replacement of SQDG at a site near the head of QB provides a possible explanation for the QB impairment. The replacement of two SQDGs located at the monomer–monomer interface by other lipids decreased the stability of the PSII dimer, resulting in an increase in the amount of PSII monomer in the mutant. The present results thus suggest that although SQDG binding in all of the PSII-binding sites is necessary to fully maintain the activity and stability of PSII, replacement of SQDG by other lipids can partially compensate for their functions.
UR - http://www.scopus.com/inward/record.url?scp=85054025982&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85054025982&partnerID=8YFLogxK
U2 - 10.1074/jbc.RA118.004304
DO - 10.1074/jbc.RA118.004304
M3 - Article
C2 - 30076221
AN - SCOPUS:85054025982
VL - 293
SP - 14786
EP - 14797
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 38
ER -