author_facet KOMATSU, S.
YANG, G.
HAYASHI, N.
KAKU, H.
UMEMURA, K.
IWASAKI, Y.
KOMATSU, S.
YANG, G.
HAYASHI, N.
KAKU, H.
UMEMURA, K.
IWASAKI, Y.
author KOMATSU, S.
YANG, G.
HAYASHI, N.
KAKU, H.
UMEMURA, K.
IWASAKI, Y.
spellingShingle KOMATSU, S.
YANG, G.
HAYASHI, N.
KAKU, H.
UMEMURA, K.
IWASAKI, Y.
Plant, Cell & Environment
Alterations by a defect in a rice G protein α subunit in probenazole and pathogen‐induced responses
Plant Science
Physiology
author_sort komatsu, s.
spelling KOMATSU, S. YANG, G. HAYASHI, N. KAKU, H. UMEMURA, K. IWASAKI, Y. 0140-7791 1365-3040 Wiley Plant Science Physiology http://dx.doi.org/10.1111/j.1365-3040.2004.01202.x <jats:title>ABSTRACT</jats:title><jats:p>The rice dwarf1 (<jats:italic>d1</jats:italic>) mutant, which is deficient in an <jats:italic>α</jats:italic> subunit (G<jats:italic>α</jats:italic>) of heterotrimeric G protein, was used to obtain specific evidence on the functions of G<jats:italic>α</jats:italic> protein in defence signalling in rice. Using proteome analysis, a probenazole‐inducible protein (PBZ1) was detected in the cytosolic fraction of leaf blade of the wild type, but not the <jats:italic>d1</jats:italic> mutant. After treatment with probenazol, PBZ1 reached maximal levels at 72 h in the wild type but 96 h in the <jats:italic>d1</jats:italic> mutant. The induction of PBZ1 by probenazole treatment was inhibited by protein kinase inhibitors. A 48‐kDa putative mitogen‐activated protein kinase (MAPK) and a 55‐kDa putative Ca<jats:sup>2+</jats:sup>‐dependent protein kinase (CDPK) showed lower activities in the cytosolic fraction of the <jats:italic>d1</jats:italic> mutant than that of the wild type. The activities of these protein kinases were enhanced at 24 h in the wild type and 48 h in the <jats:italic>d1</jats:italic> mutant after probenazole treatment. Although the <jats:italic>d1</jats:italic> mutant responded to the rice blast fungus similarly to the wild type, the <jats:italic>d1</jats:italic> mutant developed rice blight symptoms earlier than the wild type when infected with <jats:italic>Xoo</jats:italic>. In addition, the blight symptoms were more severe on the mutant than on the wild type, and wilting was frequently observed in the <jats:italic>d1</jats:italic> mutant. Furthermore, induction by the bacterial infection of the 48‐kDa putative MAPK and PBZ1 was delayed by 2 and 4 d, respectively, in the <jats:italic>d1</jats:italic> mutant compared with the wild type. These results indicate that the G<jats:italic>α</jats:italic> protein plays a role in the induction of PBZ1 and protein kinases by probenazole and <jats:italic>Xoo</jats:italic>, and suggest that the 48‐kDa putative MAPK may be involved in a signalling pathway for resistance to bacterial infection.</jats:p> Alterations by a defect in a rice G protein <i>α</i> subunit in probenazole and pathogen‐induced responses Plant, Cell & Environment
doi_str_mv 10.1111/j.1365-3040.2004.01202.x
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DE-14
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imprint_str_mv Wiley, 2004
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recordtype ai
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series Plant, Cell & Environment
source_id 49
title Alterations by a defect in a rice G protein α subunit in probenazole and pathogen‐induced responses
title_unstemmed Alterations by a defect in a rice G protein α subunit in probenazole and pathogen‐induced responses
title_full Alterations by a defect in a rice G protein α subunit in probenazole and pathogen‐induced responses
title_fullStr Alterations by a defect in a rice G protein α subunit in probenazole and pathogen‐induced responses
title_full_unstemmed Alterations by a defect in a rice G protein α subunit in probenazole and pathogen‐induced responses
title_short Alterations by a defect in a rice G protein α subunit in probenazole and pathogen‐induced responses
title_sort alterations by a defect in a rice g protein <i>α</i> subunit in probenazole and pathogen‐induced responses
topic Plant Science
Physiology
url http://dx.doi.org/10.1111/j.1365-3040.2004.01202.x
publishDate 2004
physical 947-957
description <jats:title>ABSTRACT</jats:title><jats:p>The rice dwarf1 (<jats:italic>d1</jats:italic>) mutant, which is deficient in an <jats:italic>α</jats:italic> subunit (G<jats:italic>α</jats:italic>) of heterotrimeric G protein, was used to obtain specific evidence on the functions of G<jats:italic>α</jats:italic> protein in defence signalling in rice. Using proteome analysis, a probenazole‐inducible protein (PBZ1) was detected in the cytosolic fraction of leaf blade of the wild type, but not the <jats:italic>d1</jats:italic> mutant. After treatment with probenazol, PBZ1 reached maximal levels at 72 h in the wild type but 96 h in the <jats:italic>d1</jats:italic> mutant. The induction of PBZ1 by probenazole treatment was inhibited by protein kinase inhibitors. A 48‐kDa putative mitogen‐activated protein kinase (MAPK) and a 55‐kDa putative Ca<jats:sup>2+</jats:sup>‐dependent protein kinase (CDPK) showed lower activities in the cytosolic fraction of the <jats:italic>d1</jats:italic> mutant than that of the wild type. The activities of these protein kinases were enhanced at 24 h in the wild type and 48 h in the <jats:italic>d1</jats:italic> mutant after probenazole treatment. Although the <jats:italic>d1</jats:italic> mutant responded to the rice blast fungus similarly to the wild type, the <jats:italic>d1</jats:italic> mutant developed rice blight symptoms earlier than the wild type when infected with <jats:italic>Xoo</jats:italic>. In addition, the blight symptoms were more severe on the mutant than on the wild type, and wilting was frequently observed in the <jats:italic>d1</jats:italic> mutant. Furthermore, induction by the bacterial infection of the 48‐kDa putative MAPK and PBZ1 was delayed by 2 and 4 d, respectively, in the <jats:italic>d1</jats:italic> mutant compared with the wild type. These results indicate that the G<jats:italic>α</jats:italic> protein plays a role in the induction of PBZ1 and protein kinases by probenazole and <jats:italic>Xoo</jats:italic>, and suggest that the 48‐kDa putative MAPK may be involved in a signalling pathway for resistance to bacterial infection.</jats:p>
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author KOMATSU, S., YANG, G., HAYASHI, N., KAKU, H., UMEMURA, K., IWASAKI, Y.
author_facet KOMATSU, S., YANG, G., HAYASHI, N., KAKU, H., UMEMURA, K., IWASAKI, Y., KOMATSU, S., YANG, G., HAYASHI, N., KAKU, H., UMEMURA, K., IWASAKI, Y.
author_sort komatsu, s.
container_issue 7
container_start_page 947
container_title Plant, Cell & Environment
container_volume 27
description <jats:title>ABSTRACT</jats:title><jats:p>The rice dwarf1 (<jats:italic>d1</jats:italic>) mutant, which is deficient in an <jats:italic>α</jats:italic> subunit (G<jats:italic>α</jats:italic>) of heterotrimeric G protein, was used to obtain specific evidence on the functions of G<jats:italic>α</jats:italic> protein in defence signalling in rice. Using proteome analysis, a probenazole‐inducible protein (PBZ1) was detected in the cytosolic fraction of leaf blade of the wild type, but not the <jats:italic>d1</jats:italic> mutant. After treatment with probenazol, PBZ1 reached maximal levels at 72 h in the wild type but 96 h in the <jats:italic>d1</jats:italic> mutant. The induction of PBZ1 by probenazole treatment was inhibited by protein kinase inhibitors. A 48‐kDa putative mitogen‐activated protein kinase (MAPK) and a 55‐kDa putative Ca<jats:sup>2+</jats:sup>‐dependent protein kinase (CDPK) showed lower activities in the cytosolic fraction of the <jats:italic>d1</jats:italic> mutant than that of the wild type. The activities of these protein kinases were enhanced at 24 h in the wild type and 48 h in the <jats:italic>d1</jats:italic> mutant after probenazole treatment. Although the <jats:italic>d1</jats:italic> mutant responded to the rice blast fungus similarly to the wild type, the <jats:italic>d1</jats:italic> mutant developed rice blight symptoms earlier than the wild type when infected with <jats:italic>Xoo</jats:italic>. In addition, the blight symptoms were more severe on the mutant than on the wild type, and wilting was frequently observed in the <jats:italic>d1</jats:italic> mutant. Furthermore, induction by the bacterial infection of the 48‐kDa putative MAPK and PBZ1 was delayed by 2 and 4 d, respectively, in the <jats:italic>d1</jats:italic> mutant compared with the wild type. These results indicate that the G<jats:italic>α</jats:italic> protein plays a role in the induction of PBZ1 and protein kinases by probenazole and <jats:italic>Xoo</jats:italic>, and suggest that the 48‐kDa putative MAPK may be involved in a signalling pathway for resistance to bacterial infection.</jats:p>
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imprint Wiley, 2004
imprint_str_mv Wiley, 2004
institution DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Rs1, DE-Pl11
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spelling KOMATSU, S. YANG, G. HAYASHI, N. KAKU, H. UMEMURA, K. IWASAKI, Y. 0140-7791 1365-3040 Wiley Plant Science Physiology http://dx.doi.org/10.1111/j.1365-3040.2004.01202.x <jats:title>ABSTRACT</jats:title><jats:p>The rice dwarf1 (<jats:italic>d1</jats:italic>) mutant, which is deficient in an <jats:italic>α</jats:italic> subunit (G<jats:italic>α</jats:italic>) of heterotrimeric G protein, was used to obtain specific evidence on the functions of G<jats:italic>α</jats:italic> protein in defence signalling in rice. Using proteome analysis, a probenazole‐inducible protein (PBZ1) was detected in the cytosolic fraction of leaf blade of the wild type, but not the <jats:italic>d1</jats:italic> mutant. After treatment with probenazol, PBZ1 reached maximal levels at 72 h in the wild type but 96 h in the <jats:italic>d1</jats:italic> mutant. The induction of PBZ1 by probenazole treatment was inhibited by protein kinase inhibitors. A 48‐kDa putative mitogen‐activated protein kinase (MAPK) and a 55‐kDa putative Ca<jats:sup>2+</jats:sup>‐dependent protein kinase (CDPK) showed lower activities in the cytosolic fraction of the <jats:italic>d1</jats:italic> mutant than that of the wild type. The activities of these protein kinases were enhanced at 24 h in the wild type and 48 h in the <jats:italic>d1</jats:italic> mutant after probenazole treatment. Although the <jats:italic>d1</jats:italic> mutant responded to the rice blast fungus similarly to the wild type, the <jats:italic>d1</jats:italic> mutant developed rice blight symptoms earlier than the wild type when infected with <jats:italic>Xoo</jats:italic>. In addition, the blight symptoms were more severe on the mutant than on the wild type, and wilting was frequently observed in the <jats:italic>d1</jats:italic> mutant. Furthermore, induction by the bacterial infection of the 48‐kDa putative MAPK and PBZ1 was delayed by 2 and 4 d, respectively, in the <jats:italic>d1</jats:italic> mutant compared with the wild type. These results indicate that the G<jats:italic>α</jats:italic> protein plays a role in the induction of PBZ1 and protein kinases by probenazole and <jats:italic>Xoo</jats:italic>, and suggest that the 48‐kDa putative MAPK may be involved in a signalling pathway for resistance to bacterial infection.</jats:p> Alterations by a defect in a rice G protein <i>α</i> subunit in probenazole and pathogen‐induced responses Plant, Cell & Environment
spellingShingle KOMATSU, S., YANG, G., HAYASHI, N., KAKU, H., UMEMURA, K., IWASAKI, Y., Plant, Cell & Environment, Alterations by a defect in a rice G protein α subunit in probenazole and pathogen‐induced responses, Plant Science, Physiology
title Alterations by a defect in a rice G protein α subunit in probenazole and pathogen‐induced responses
title_full Alterations by a defect in a rice G protein α subunit in probenazole and pathogen‐induced responses
title_fullStr Alterations by a defect in a rice G protein α subunit in probenazole and pathogen‐induced responses
title_full_unstemmed Alterations by a defect in a rice G protein α subunit in probenazole and pathogen‐induced responses
title_short Alterations by a defect in a rice G protein α subunit in probenazole and pathogen‐induced responses
title_sort alterations by a defect in a rice g protein <i>α</i> subunit in probenazole and pathogen‐induced responses
title_unstemmed Alterations by a defect in a rice G protein α subunit in probenazole and pathogen‐induced responses
topic Plant Science, Physiology
url http://dx.doi.org/10.1111/j.1365-3040.2004.01202.x