TY - CHAP
T1 - Metal and serine proteases in the crude photosystem II particles from a diatom, Chaetoceros gracilis
AU - Nagao, Ryo
AU - Noguchi, Eri
AU - Tomo, Tatsuya
AU - Enami, Isao
AU - Ikeuchi, Masahiko
N1 - Funding Information:
This work was supported in part by Grants-in-aid for Scientific Research from the Ministry of Education of Japan 18570049 (to I. E.) and 21570038 and 22370017 (to T. T.), and Research Fellow (to R. N.) from the Japan Society for the Promotion of Science.
Funding Information:
This work was supported in part by Grants-in-aid for Scientific Research from the Ministry of Education of Japan18570049 (to I. E.) and 21570038 and 22370017 (to T. T.), and Research Fellow (to R. N.) from the Japan Society for the Promotion of Science.
Publisher Copyright:
© Zhejiang University Press, Hangzhou and Springer-Verlag Berlin Heidelberg 2013.
PY - 2013
Y1 - 2013
N2 - We found that most of subunits in crude Photosystem II particles (crude PSII) from a marine centric diatom, Chaetoceros gracilis, were degraded during incubation for 18 h at 25 °C in the dark (Nagao et al., 2010). In this study, we attempted to suppress the protein degradation by addition of protease inhibitors to the crude PSII during incubation for various times at 25 °C in the dark. When no proteases inhibitor added to the crude PSII, fucoxanthin chlorophyll a/c-binding protein (FCP), especially upper subunits of FCP, were first degraded, followed by most of PSII subunits. The degradation was slightly suppressed by a metal protease inhibitor, EDTA, or a serine protease inhibitor, PMSF, and the proteolysis activity of metal protease is slightly stronger than that of serine protease. On the other hand, the significant suppression was observed only by both EDTA and PMSF. These results suggest that the metal and serine proteases are associated with the crude PSII and the primary target of the proteases is the upper subunits of FCP.
AB - We found that most of subunits in crude Photosystem II particles (crude PSII) from a marine centric diatom, Chaetoceros gracilis, were degraded during incubation for 18 h at 25 °C in the dark (Nagao et al., 2010). In this study, we attempted to suppress the protein degradation by addition of protease inhibitors to the crude PSII during incubation for various times at 25 °C in the dark. When no proteases inhibitor added to the crude PSII, fucoxanthin chlorophyll a/c-binding protein (FCP), especially upper subunits of FCP, were first degraded, followed by most of PSII subunits. The degradation was slightly suppressed by a metal protease inhibitor, EDTA, or a serine protease inhibitor, PMSF, and the proteolysis activity of metal protease is slightly stronger than that of serine protease. On the other hand, the significant suppression was observed only by both EDTA and PMSF. These results suggest that the metal and serine proteases are associated with the crude PSII and the primary target of the proteases is the upper subunits of FCP.
KW - Chaetoceros gracilis
KW - Photosystem II
KW - Protease
KW - Proteolysis
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U2 - 10.1007/978-3-642-32034-7_18
DO - 10.1007/978-3-642-32034-7_18
M3 - Chapter
AN - SCOPUS:85060673702
T3 - Advanced Topics in Science and Technology in China
SP - 83
EP - 85
BT - Advanced Topics in Science and Technology in China
PB - Springer Science and Business Media Deutschland GmbH
ER -
