TY - JOUR
T1 - The cationic cell-wall-peroxidase having oxidation ability for polymeric substrate participates in the late stage of lignification of Populus alba L
AU - Sasaki, Shinya
AU - Baba, Kei'ichi
AU - Nishida, Tomoaki
AU - Tsutsumi, Yuji
AU - Kondo, Ryuichiro
N1 - Funding Information:
Acknowledgements We are grateful to Dr. Kazutoshi Sayama and Mr. Naoto Ogawa, Shizuoka University for technical advice on the preparation of CWPO-C antiserum. We also thank Dr. Mitsuhiro Furuse and Dr. Hironori Ando, Kyushu University for technical support regarding Real-time PCR analysis using Line Gene. This work was supported by a grant-in-aid for scientific research fund from the Ministry of Education, Science and Culture of Japan (15380121).
PY - 2006/12
Y1 - 2006/12
N2 - Previously we reported that purified Cell Wall Peroxidase-Cationic (CWPO-C) from poplar callus (Populus alba L.) oxidizes sinapyl alcohol and polymeric substrate unlike other plant peroxidases and proposed that this isoenzyme is a conceivable lignification specific peroxidase. In this study, we cloned full-length cDNA of CWPO-C and investigated the transcription of CWPO-C gene in various organs and the localization of CWPO-C protein in the differentiating xylem of poplar stem. Real-time PCR analyses indicated that CWPO-C gene is constitutively expressed in the developing xylem, leaf, and shoot but not affected by many stress treatments. Immunohistochemical analysis showed that CWPO-C locates in the middle lamellae, cell corners, and secondary cell walls of the fiber cells during the lignification. The intensity of the CWPO-C labeling increased gradually from the cell wall thickening stage to mature stage of fiber cells, which is very consistent with the increase of lignin content in the developing xylem. These results strongly support that CWPO-C is responsible for the lignification of the secondary xylem. Interestingly, immuno-labeling of CWPO-C was also observed inside of the ray parenchyma cells instead no signals were detected within the developing fiber cells. This suggests that CWPO-C is biosynthesized in the parenchyma cells and provided to the middle lamellae, the cell corners, and the cell walls to achieve lignin polymerization.
AB - Previously we reported that purified Cell Wall Peroxidase-Cationic (CWPO-C) from poplar callus (Populus alba L.) oxidizes sinapyl alcohol and polymeric substrate unlike other plant peroxidases and proposed that this isoenzyme is a conceivable lignification specific peroxidase. In this study, we cloned full-length cDNA of CWPO-C and investigated the transcription of CWPO-C gene in various organs and the localization of CWPO-C protein in the differentiating xylem of poplar stem. Real-time PCR analyses indicated that CWPO-C gene is constitutively expressed in the developing xylem, leaf, and shoot but not affected by many stress treatments. Immunohistochemical analysis showed that CWPO-C locates in the middle lamellae, cell corners, and secondary cell walls of the fiber cells during the lignification. The intensity of the CWPO-C labeling increased gradually from the cell wall thickening stage to mature stage of fiber cells, which is very consistent with the increase of lignin content in the developing xylem. These results strongly support that CWPO-C is responsible for the lignification of the secondary xylem. Interestingly, immuno-labeling of CWPO-C was also observed inside of the ray parenchyma cells instead no signals were detected within the developing fiber cells. This suggests that CWPO-C is biosynthesized in the parenchyma cells and provided to the middle lamellae, the cell corners, and the cell walls to achieve lignin polymerization.
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U2 - 10.1007/s11103-006-9057-3
DO - 10.1007/s11103-006-9057-3
M3 - Article
C2 - 17004015
AN - SCOPUS:33750898437
SN - 0167-4412
VL - 62
SP - 797
EP - 807
JO - Plant Molecular Biology
JF - Plant Molecular Biology
IS - 6
ER -