TY - JOUR
T1 - Association of small CAB-like proteins (SCPs) of Synechocystis sp. PCC 6803 with Photosystem II
AU - Kufryk, Galyna
AU - Hernandez-Prieto, Miguel A.
AU - Kieselbach, Thomas
AU - Miranda, Helder
AU - Vermaas, Willem
AU - Funk, Christiane
N1 - Funding Information:
Acknowledgments The authors would like to thank the Swedish Foundation for International Cooperation in Research and Higher Education (STINT) for supporting the collaboration between the two research groups. C.F. is very grateful to the Royal Swedish Academy of Sciences (KVA) for granting her research position and to the Swedish Research Council (VR) for financial support. W.V. acknowledges research grant support from the US Department of Energy (DE-FG02-04ER15543).
PY - 2008/2
Y1 - 2008/2
N2 - The cyanobacterial small CAB-like proteins (SCPs) are one-helix proteins with compelling similarity to the first and third transmembrane helix of proteins belonging to the CAB family of light-harvesting complex proteins in plants. The SCP proteins are transiently expressed at high light intensity and other stress conditions but their exact function remains largely unknown. Recently we showed association of ScpD with light-stressed, monomeric Photosystem II in Synechocystis sp. PCC 6803 (Yao et al. J Biol Chem 282:267-276, 2007). Here we show that ScpB associates with Photosystem II at normal growth conditions. Moreover, upon introduction of a construct into Synechocystis so that ScpB is expressed continuously under normal growth conditions, ScpE was detected under non-stressed conditions as well, and was copurified with tagged ScpB and Photosystem II. We also report on a one-helix protein, Slr1544, that is somewhat similar to the SCPs and whose gene is cotranscribed with that of ScpD; Slr1544 is another member of the extended light-harvesting-like (Lil) protein family, and we propose to name it LilA.
AB - The cyanobacterial small CAB-like proteins (SCPs) are one-helix proteins with compelling similarity to the first and third transmembrane helix of proteins belonging to the CAB family of light-harvesting complex proteins in plants. The SCP proteins are transiently expressed at high light intensity and other stress conditions but their exact function remains largely unknown. Recently we showed association of ScpD with light-stressed, monomeric Photosystem II in Synechocystis sp. PCC 6803 (Yao et al. J Biol Chem 282:267-276, 2007). Here we show that ScpB associates with Photosystem II at normal growth conditions. Moreover, upon introduction of a construct into Synechocystis so that ScpB is expressed continuously under normal growth conditions, ScpE was detected under non-stressed conditions as well, and was copurified with tagged ScpB and Photosystem II. We also report on a one-helix protein, Slr1544, that is somewhat similar to the SCPs and whose gene is cotranscribed with that of ScpD; Slr1544 is another member of the extended light-harvesting-like (Lil) protein family, and we propose to name it LilA.
KW - Antenna
KW - Chlorophyll-binding protein
KW - Cyanobacteria
KW - Early-light induced proteins (ELIPs)
KW - High-light induced proteins (HLIPs)
KW - Light-harvesting complex
KW - Synechocystis sp. PCC 6803
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U2 - 10.1007/s11120-007-9244-3
DO - 10.1007/s11120-007-9244-3
M3 - Article
C2 - 17912610
AN - SCOPUS:37749002134
SN - 0166-8595
VL - 95
SP - 135
EP - 145
JO - Photosynthesis research
JF - Photosynthesis research
IS - 2-3
ER -