PubMed:28751317
Annnotations
pqqtest_sentence
{"project":"pqqtest_sentence","denotations":[{"id":"M_0","span":{"begin":638,"end":666},"obj":"cand:TO:0000467-cell membrane stability"},{"id":"M_1","span":{"begin":638,"end":666},"obj":"cand:PO:0025028-embryo plant cell"},{"id":"M_2","span":{"begin":638,"end":666},"obj":"cand:TO:0000325-soluble protein content"},{"id":"M_3","span":{"begin":638,"end":666},"obj":"cand:PECO:0007266-in vitro growth medium exposure"},{"id":"M_4","span":{"begin":638,"end":666},"obj":"cand:PO:0000004-in vitro plant structure"},{"id":"M_5","span":{"begin":638,"end":666},"obj":"cand:TO:0000324-rubisco to soluble protein ratio"},{"id":"M_6","span":{"begin":638,"end":666},"obj":"cand:PO:0007057-seed germination stage"},{"id":"M_7","span":{"begin":638,"end":666},"obj":"cand:funRiceGene:410-cell fate transition"},{"id":"M_8","span":{"begin":638,"end":666},"obj":"cand:funRiceGene:227-cell elongation"},{"id":"M_9","span":{"begin":638,"end":666},"obj":"cand:funRiceGene:27-cell 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REGULATOR OF IRON HOMEOSTASIS 1 (OsPRI1) positively regulates iron homeostasis in rice.\nOsHRZ1 is a potential iron-binding sensor. However, it is unclear how OsHRZ1 transmits signals. In this study, we reveal that OsPRI1 interacts with OsHRZ1. A loss-of-function mutation to OsPRI1 increased the sensitivity of plants to Fe-deficient conditions and downregulated the expression of Fe-deficiency-responsive genes. Yeast one-hybrid and electrophoretic mobility shift assay results suggested that OsPRI1 binds to the OsIRO2 and OsIRO3 promoters. In vitro ubiquitination experiments indicated that OsPRI1 is ubiquitinated by OsHRZ1. Cell-free degradation assays revealed that the stability of OsPRI1 decreased in wild type roots, but increased in the hrz1-2 mutant, suggesting OsHRZ1 is responsible for the instability of OsPRI1. The hrz1-2 seedlings were insensitive to Fe-deficient conditions. When the pri1-1 mutation was introduced into hrz1-2 mutants, the pri1hrz1 double mutant was more sensitive to Fe deficiency than the hrz1-2 mutant. Additionally, the expression levels of Fe-deficiency-responsive genes were lower in the hrz1pri1 double mutant than in the hrz1-2 mutant. Collectively, these results imply that OsPRI1, which is ubiquitinated by OsHRZ1, mediates rice responses to Fe-deficiency by positively regulating OsIRO2 and OsIRO3 expression as part of the OsHRZ1-OsPRI1-OsIRO2/3 signal transduction cascade."}
21k_plant_trait_mention
{"project":"21k_plant_trait_mention","denotations":[{"id":"M_0","span":{"begin":1401,"end":1420},"obj":"funRiceGene:486, xzyao:14470"},{"id":"M_1","span":{"begin":846,"end":855},"obj":"funRiceGene:507"},{"id":"M_3","span":{"begin":1011,"end":1013},"obj":"funRiceGene:50"},{"id":"M_4","span":{"begin":1295,"end":1297},"obj":"funRiceGene:50"},{"id":"M_6","span":{"begin":756,"end":762},"obj":"hunflair:NA:Gene"},{"id":"M_7","span":{"begin":839,"end":845},"obj":"hunflair:NA:Gene"},{"id":"M_8","span":{"begin":946,"end":952},"obj":"hunflair:NA:Gene"},{"id":"M_9","span":{"begin":1034,"end":1040},"obj":"hunflair:NA:Gene"},{"id":"M_10","span":{"begin":1172,"end":1178},"obj":"hunflair:NA:Gene"},{"id":"M_13","span":{"begin":245,"end":251},"obj":"hunflair:NA:Gene"},{"id":"M_14","span":{"begin":630,"end":636},"obj":"hunflair:NA:Gene"},{"id":"M_15","span":{"begin":782,"end":788},"obj":"hunflair:NA:Gene"},{"id":"M_16","span":{"begin":1260,"end":1266},"obj":"hunflair:NA:Gene"},{"id":"M_17","span":{"begin":1378,"end":1384},"obj":"hunflair:NA:Gene"},{"id":"M_18","span":{"begin":1378,"end":1400},"obj":"hunflair:NA:Gene"},{"id":"M_21","span":{"begin":1137,"end":1145},"obj":"hunflair:NA:Gene"},{"id":"M_24","span":{"begin":523,"end":529},"obj":"hunflair:NA:Gene"},{"id":"M_25","span":{"begin":1334,"end":1340},"obj":"hunflair:NA:Gene"},{"id":"M_26","span":{"begin":1392,"end":1398},"obj":"hunflair:NA:Gene"},{"id":"M_27","span":{"begin":22,"end":26},"obj":"hunflair:NA:Chemical"},{"id":"M_29","span":{"begin":910,"end":916},"obj":"hunflair:NA:Gene"},{"id":"M_30","span":{"begin":1011,"end":1024},"obj":"hunflair:NA:Disease"},{"id":"M_31","span":{"begin":1295,"end":1308},"obj":"hunflair:NA:Disease"},{"id":"M_32","span":{"begin":756,"end":762},"obj":"hunflair:NA:CellLine"},{"id":"M_33","span":{"begin":839,"end":845},"obj":"hunflair:NA:CellLine"},{"id":"M_34","span":{"begin":946,"end":952},"obj":"hunflair:NA:CellLine"},{"id":"M_35","span":{"begin":1034,"end":1040},"obj":"hunflair:NA:CellLine"},{"id":"M_36","span":{"begin":1172,"end":1178},"obj":"hunflair:NA:CellLine"},{"id":"M_38","span":{"begin":42,"end":48},"obj":"hunflair:NA:Gene"},{"id":"M_39","span":{"begin":284,"end":290},"obj":"hunflair:NA:Gene"},{"id":"M_40","span":{"begin":503,"end":509},"obj":"hunflair:NA:Gene"},{"id":"M_41","span":{"begin":603,"end":609},"obj":"hunflair:NA:Gene"},{"id":"M_42","span":{"begin":698,"end":704},"obj":"hunflair:NA:Gene"},{"id":"M_43","span":{"begin":827,"end":833},"obj":"hunflair:NA:Gene"},{"id":"M_44","span":{"begin":1226,"end":1232},"obj":"hunflair:NA:Gene"},{"id":"M_45","span":{"begin":1385,"end":1391},"obj":"hunflair:NA:Gene"},{"id":"M_46","span":{"begin":534,"end":540},"obj":"hunflair:NA:Gene"},{"id":"M_47","span":{"begin":1345,"end":1351},"obj":"hunflair:NA:Gene"},{"id":"M_49","span":{"begin":966,"end":974},"obj":"hunflair:NA:Gene"},{"id":"M_50","span":{"begin":1277,"end":1281},"obj":"hunflair:NA:Species"},{"id":"M_51","span":{"begin":330,"end":332},"obj":"hunflair:NA:Chemical"},{"id":"M_52","span":{"begin":390,"end":392},"obj":"hunflair:NA:Chemical"},{"id":"M_53","span":{"begin":876,"end":878},"obj":"hunflair:NA:Chemical"},{"id":"M_54","span":{"begin":1011,"end":1013},"obj":"hunflair:NA:Chemical"},{"id":"M_55","span":{"begin":1088,"end":1090},"obj":"hunflair:NA:Chemical"},{"id":"M_56","span":{"begin":1295,"end":1297},"obj":"hunflair:NA:Chemical"},{"id":"M_58","span":{"begin":330,"end":332},"obj":"pubtator:MESH:D007501:Chemical"},{"id":"M_59","span":{"begin":390,"end":392},"obj":"pubtator:MESH:D007501:Chemical"},{"id":"M_60","span":{"begin":876,"end":878},"obj":"pubtator:MESH:D007501:Chemical"},{"id":"M_61","span":{"begin":1011,"end":1013},"obj":"pubtator:MESH:D007501:Chemical"},{"id":"M_62","span":{"begin":1088,"end":1090},"obj":"pubtator:MESH:D007501:Chemical"},{"id":"M_63","span":{"begin":1295,"end":1297},"obj":"pubtator:MESH:D007501:Chemical"},{"id":"M_65","span":{"begin":422,"end":427},"obj":"pubtator:4932:Species"},{"id":"M_66","span":{"begin":330,"end":353},"obj":"pubtator:MESH:D009135:Disease"},{"id":"M_67","span":{"begin":876,"end":899},"obj":"pubtator:MESH:D009135:Disease"},{"id":"M_68","span":{"begin":1277,"end":1281},"obj":"pubtator:4530:Species"},{"id":"M_70","span":{"begin":1011,"end":1024},"obj":"pubtator::Disease"},{"id":"M_71","span":{"begin":1295,"end":1308},"obj":"pubtator::Disease"}],"text":"POSITIVE REGULATOR OF IRON HOMEOSTASIS 1 (OsPRI1) positively regulates iron homeostasis in rice.\nOsHRZ1 is a potential iron-binding sensor. However, it is unclear how OsHRZ1 transmits signals. In this study, we reveal that OsPRI1 interacts with OsHRZ1. A loss-of-function mutation to OsPRI1 increased the sensitivity of plants to Fe-deficient conditions and downregulated the expression of Fe-deficiency-responsive genes. Yeast one-hybrid and electrophoretic mobility shift assay results suggested that OsPRI1 binds to the OsIRO2 and OsIRO3 promoters. In vitro ubiquitination experiments indicated that OsPRI1 is ubiquitinated by OsHRZ1. Cell-free degradation assays revealed that the stability of OsPRI1 decreased in wild type roots, but increased in the hrz1-2 mutant, suggesting OsHRZ1 is responsible for the instability of OsPRI1. The hrz1-2 seedlings were insensitive to Fe-deficient conditions. When the pri1-1 mutation was introduced into hrz1-2 mutants, the pri1hrz1 double mutant was more sensitive to Fe deficiency than the hrz1-2 mutant. Additionally, the expression levels of Fe-deficiency-responsive genes were lower in the hrz1pri1 double mutant than in the hrz1-2 mutant. Collectively, these results imply that OsPRI1, which is ubiquitinated by OsHRZ1, mediates rice responses to Fe-deficiency by positively regulating OsIRO2 and OsIRO3 expression as part of the OsHRZ1-OsPRI1-OsIRO2/3 signal transduction cascade."}
OryzaGP_2022
{"project":"OryzaGP_2022","denotations":[{"id":"T1","span":{"begin":39,"end":40},"obj":"http://identifiers.org/oryzabase.gene/11216"},{"id":"T2","span":{"begin":915,"end":916},"obj":"http://identifiers.org/oryzabase.gene/11216"}],"text":"POSITIVE REGULATOR OF IRON HOMEOSTASIS 1 (OsPRI1) positively regulates iron homeostasis in rice.\nOsHRZ1 is a potential iron-binding sensor. However, it is unclear how OsHRZ1 transmits signals. In this study, we reveal that OsPRI1 interacts with OsHRZ1. A loss-of-function mutation to OsPRI1 increased the sensitivity of plants to Fe-deficient conditions and downregulated the expression of Fe-deficiency-responsive genes. Yeast one-hybrid and electrophoretic mobility shift assay results suggested that OsPRI1 binds to the OsIRO2 and OsIRO3 promoters. In vitro ubiquitination experiments indicated that OsPRI1 is ubiquitinated by OsHRZ1. Cell-free degradation assays revealed that the stability of OsPRI1 decreased in wild type roots, but increased in the hrz1-2 mutant, suggesting OsHRZ1 is responsible for the instability of OsPRI1. The hrz1-2 seedlings were insensitive to Fe-deficient conditions. When the pri1-1 mutation was introduced into hrz1-2 mutants, the pri1hrz1 double mutant was more sensitive to Fe deficiency than the hrz1-2 mutant. Additionally, the expression levels of Fe-deficiency-responsive genes were lower in the hrz1pri1 double mutant than in the hrz1-2 mutant. Collectively, these results imply that OsPRI1, which is ubiquitinated by OsHRZ1, mediates rice responses to Fe-deficiency by positively regulating OsIRO2 and OsIRO3 expression as part of the OsHRZ1-OsPRI1-OsIRO2/3 signal transduction cascade."}
OryzaGP_2021_v2
{"project":"OryzaGP_2021_v2","denotations":[{"id":"T1","span":{"begin":42,"end":48},"obj":"http://identifiers.org/oryzabase.gene/15350"},{"id":"T2","span":{"begin":97,"end":103},"obj":"http://identifiers.org/oryzabase.gene/15055"},{"id":"T3","span":{"begin":167,"end":173},"obj":"http://identifiers.org/oryzabase.gene/15055"},{"id":"T4","span":{"begin":223,"end":229},"obj":"http://identifiers.org/oryzabase.gene/15350"},{"id":"T5","span":{"begin":245,"end":251},"obj":"http://identifiers.org/oryzabase.gene/15055"},{"id":"T6","span":{"begin":284,"end":290},"obj":"http://identifiers.org/oryzabase.gene/15350"},{"id":"T7","span":{"begin":503,"end":509},"obj":"http://identifiers.org/oryzabase.gene/15350"},{"id":"T8","span":{"begin":523,"end":529},"obj":"http://identifiers.org/oryzabase.gene/9483"},{"id":"T9","span":{"begin":534,"end":540},"obj":"http://identifiers.org/oryzabase.gene/11136"},{"id":"T10","span":{"begin":603,"end":609},"obj":"http://identifiers.org/oryzabase.gene/15350"},{"id":"T11","span":{"begin":630,"end":636},"obj":"http://identifiers.org/oryzabase.gene/15055"},{"id":"T12","span":{"begin":698,"end":704},"obj":"http://identifiers.org/oryzabase.gene/15350"},{"id":"T13","span":{"begin":782,"end":788},"obj":"http://identifiers.org/oryzabase.gene/15055"},{"id":"T14","span":{"begin":827,"end":833},"obj":"http://identifiers.org/oryzabase.gene/15350"},{"id":"T15","span":{"begin":1226,"end":1232},"obj":"http://identifiers.org/oryzabase.gene/15350"},{"id":"T16","span":{"begin":1260,"end":1266},"obj":"http://identifiers.org/oryzabase.gene/15055"},{"id":"T17","span":{"begin":1334,"end":1340},"obj":"http://identifiers.org/oryzabase.gene/9483"},{"id":"T18","span":{"begin":1345,"end":1351},"obj":"http://identifiers.org/oryzabase.gene/11136"},{"id":"T19","span":{"begin":1378,"end":1384},"obj":"http://identifiers.org/oryzabase.gene/15055"},{"id":"T20","span":{"begin":1385,"end":1391},"obj":"http://identifiers.org/oryzabase.gene/15350"},{"id":"T21","span":{"begin":1392,"end":1398},"obj":"http://identifiers.org/oryzabase.gene/9483"},{"id":"T16542","span":{"begin":42,"end":48},"obj":"http://identifiers.org/rapdb.locus/Os08g0138500"},{"id":"T34376","span":{"begin":97,"end":103},"obj":"http://identifiers.org/rapdb.locus/Os01g0689451"},{"id":"T83900","span":{"begin":167,"end":173},"obj":"http://identifiers.org/rapdb.locus/Os01g0689451"},{"id":"T73746","span":{"begin":223,"end":229},"obj":"http://identifiers.org/rapdb.locus/Os08g0138500"},{"id":"T95055","span":{"begin":245,"end":251},"obj":"http://identifiers.org/rapdb.locus/Os01g0689451"},{"id":"T25535","span":{"begin":284,"end":290},"obj":"http://identifiers.org/rapdb.locus/Os08g0138500"},{"id":"T94260","span":{"begin":503,"end":509},"obj":"http://identifiers.org/rapdb.locus/Os08g0138500"},{"id":"T65091","span":{"begin":523,"end":529},"obj":"http://identifiers.org/rapdb.locus/Os01g0952800"},{"id":"T2879","span":{"begin":534,"end":540},"obj":"http://identifiers.org/rapdb.locus/Os03g0379300"},{"id":"T17655","span":{"begin":603,"end":609},"obj":"http://identifiers.org/rapdb.locus/Os08g0138500"},{"id":"T16270","span":{"begin":630,"end":636},"obj":"http://identifiers.org/rapdb.locus/Os01g0689451"},{"id":"T70379","span":{"begin":698,"end":704},"obj":"http://identifiers.org/rapdb.locus/Os08g0138500"},{"id":"T255","span":{"begin":782,"end":788},"obj":"http://identifiers.org/rapdb.locus/Os01g0689451"},{"id":"T20882","span":{"begin":827,"end":833},"obj":"http://identifiers.org/rapdb.locus/Os08g0138500"},{"id":"T57896","span":{"begin":1226,"end":1232},"obj":"http://identifiers.org/rapdb.locus/Os08g0138500"},{"id":"T48395","span":{"begin":1260,"end":1266},"obj":"http://identifiers.org/rapdb.locus/Os01g0689451"},{"id":"T12074","span":{"begin":1334,"end":1340},"obj":"http://identifiers.org/rapdb.locus/Os01g0952800"},{"id":"T81678","span":{"begin":1345,"end":1351},"obj":"http://identifiers.org/rapdb.locus/Os03g0379300"},{"id":"T41459","span":{"begin":1378,"end":1384},"obj":"http://identifiers.org/rapdb.locus/Os01g0689451"},{"id":"T32922","span":{"begin":1385,"end":1391},"obj":"http://identifiers.org/rapdb.locus/Os08g0138500"},{"id":"T23773","span":{"begin":1392,"end":1398},"obj":"http://identifiers.org/rapdb.locus/Os01g0952800"}],"text":"POSITIVE REGULATOR OF IRON HOMEOSTASIS 1 (OsPRI1) positively regulates iron homeostasis in rice.\nOsHRZ1 is a potential iron-binding sensor. However, it is unclear how OsHRZ1 transmits signals. In this study, we reveal that OsPRI1 interacts with OsHRZ1. A loss-of-function mutation to OsPRI1 increased the sensitivity of plants to Fe-deficient conditions and downregulated the expression of Fe-deficiency-responsive genes. Yeast one-hybrid and electrophoretic mobility shift assay results suggested that OsPRI1 binds to the OsIRO2 and OsIRO3 promoters. In vitro ubiquitination experiments indicated that OsPRI1 is ubiquitinated by OsHRZ1. Cell-free degradation assays revealed that the stability of OsPRI1 decreased in wild type roots, but increased in the hrz1-2 mutant, suggesting OsHRZ1 is responsible for the instability of OsPRI1. The hrz1-2 seedlings were insensitive to Fe-deficient conditions. When the pri1-1 mutation was introduced into hrz1-2 mutants, the pri1hrz1 double mutant was more sensitive to Fe deficiency than the hrz1-2 mutant. Additionally, the expression levels of Fe-deficiency-responsive genes were lower in the hrz1pri1 double mutant than in the hrz1-2 mutant. Collectively, these results imply that OsPRI1, which is ubiquitinated by OsHRZ1, mediates rice responses to Fe-deficiency by positively regulating OsIRO2 and OsIRO3 expression as part of the OsHRZ1-OsPRI1-OsIRO2/3 signal transduction cascade."}
OryzaGP_2021_FLAIR
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OryzaGP_2021
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{"begin":1295,"end":1297},"obj":"hunflair:NA:Chemical"}],"text":"POSITIVE REGULATOR OF IRON HOMEOSTASIS 1 (OsPRI1) positively regulates iron homeostasis in rice.\nOsHRZ1 is a potential iron-binding sensor. However, it is unclear how OsHRZ1 transmits signals. In this study, we reveal that OsPRI1 interacts with OsHRZ1. A loss-of-function mutation to OsPRI1 increased the sensitivity of plants to Fe-deficient conditions and downregulated the expression of Fe-deficiency-responsive genes. Yeast one-hybrid and electrophoretic mobility shift assay results suggested that OsPRI1 binds to the OsIRO2 and OsIRO3 promoters. In vitro ubiquitination experiments indicated that OsPRI1 is ubiquitinated by OsHRZ1. Cell-free degradation assays revealed that the stability of OsPRI1 decreased in wild type roots, but increased in the hrz1-2 mutant, suggesting OsHRZ1 is responsible for the instability of OsPRI1. The hrz1-2 seedlings were insensitive to Fe-deficient conditions. When the pri1-1 mutation was introduced into hrz1-2 mutants, the pri1hrz1 double mutant was more sensitive to Fe deficiency than the hrz1-2 mutant. Additionally, the expression levels of Fe-deficiency-responsive genes were lower in the hrz1pri1 double mutant than in the hrz1-2 mutant. Collectively, these results imply that OsPRI1, which is ubiquitinated by OsHRZ1, mediates rice responses to Fe-deficiency by positively regulating OsIRO2 and OsIRO3 expression as part of the OsHRZ1-OsPRI1-OsIRO2/3 signal transduction cascade."}
kaiyin_test
{"project":"kaiyin_test","denotations":[{"id":"T2","span":{"begin":255,"end":271},"obj":"NegReg"},{"id":"T3","span":{"begin":272,"end":280},"obj":"Var"},{"id":"T4","span":{"begin":284,"end":290},"obj":"Gene"},{"id":"T5","span":{"begin":291,"end":300},"obj":"PosReg"},{"id":"T6","span":{"begin":305,"end":353},"obj":"MPA"},{"id":"T7","span":{"begin":358,"end":371},"obj":"NegReg"},{"id":"T8","span":{"begin":376,"end":420},"obj":"MPA"},{"id":"T12","span":{"begin":685,"end":694},"obj":"MPA"},{"id":"T9","span":{"begin":739,"end":748},"obj":"PosReg"},{"id":"T10","span":{"begin":756,"end":762},"obj":"Gene"},{"id":"T11","span":{"begin":763,"end":769},"obj":"Var"},{"id":"T13","span":{"begin":910,"end":916},"obj":"Gene"},{"id":"T14","span":{"begin":917,"end":925},"obj":"Var"},{"id":"T15","span":{"begin":930,"end":940},"obj":"Interaction"},{"id":"T16","span":{"begin":946,"end":952},"obj":"Gene"},{"id":"T17","span":{"begin":953,"end":960},"obj":"Var"},{"id":"T18","span":{"begin":993,"end":997},"obj":"PosReg"},{"id":"T19","span":{"begin":998,"end":1024},"obj":"MPA"}],"relations":[{"id":"R1","pred":"CauseOf","subj":"T3","obj":"T2"},{"id":"R10","pred":"ThemeOf","subj":"T13","obj":"T14"},{"id":"R11","pred":"ThemeOf","subj":"T14","obj":"T15"},{"id":"R12","pred":"ThemeOf","subj":"T17","obj":"T15"},{"id":"R13","pred":"ThemeOf","subj":"T16","obj":"T17"},{"id":"R14","pred":"CauseOf","subj":"T16","obj":"T15"},{"id":"R15","pred":"CauseOf","subj":"T17","obj":"T18"},{"id":"R16","pred":"ThemeOf","subj":"T19","obj":"T18"},{"id":"R2","pred":"ThemeOf","subj":"T4","obj":"T3"},{"id":"R3","pred":"CauseOf","subj":"T3","obj":"T5"},{"id":"R4","pred":"ThemeOf","subj":"T6","obj":"T5"},{"id":"R5","pred":"CauseOf","subj":"T3","obj":"T7"},{"id":"R6","pred":"ThemeOf","subj":"T8","obj":"T7"},{"id":"R7","pred":"ThemeOf","subj":"T10","obj":"T11"},{"id":"R8","pred":"CauseOf","subj":"T11","obj":"T9"},{"id":"R9","pred":"ThemeOf","subj":"T12","obj":"T9"}],"text":"POSITIVE REGULATOR OF IRON HOMEOSTASIS 1 (OsPRI1) positively regulates iron homeostasis in rice.\nOsHRZ1 is a potential iron-binding sensor. However, it is unclear how OsHRZ1 transmits signals. In this study, we reveal that OsPRI1 interacts with OsHRZ1. A loss-of-function mutation to OsPRI1 increased the sensitivity of plants to Fe-deficient conditions and downregulated the expression of Fe-deficiency-responsive genes. Yeast one-hybrid and electrophoretic mobility shift assay results suggested that OsPRI1 binds to the OsIRO2 and OsIRO3 promoters. In vitro ubiquitination experiments indicated that OsPRI1 is ubiquitinated by OsHRZ1. Cell-free degradation assays revealed that the stability of OsPRI1 decreased in wild type roots, but increased in the hrz1-2 mutant, suggesting OsHRZ1 is responsible for the instability of OsPRI1. The hrz1-2 seedlings were insensitive to Fe-deficient conditions. When the pri1-1 mutation was introduced into hrz1-2 mutants, the pri1hrz1 double mutant was more sensitive to Fe deficiency than the hrz1-2 mutant. Additionally, the expression levels of Fe-deficiency-responsive genes were lower in the hrz1pri1 double mutant than in the hrz1-2 mutant. Collectively, these results imply that OsPRI1, which is ubiquitinated by OsHRZ1, mediates rice responses to Fe-deficiency by positively regulating OsIRO2 and OsIRO3 expression as part of the OsHRZ1-OsPRI1-OsIRO2/3 signal transduction cascade."}
name_no
{"project":"name_no","denotations":[{"id":"T2","span":{"begin":255,"end":271},"obj":"NegReg"},{"id":"T3","span":{"begin":272,"end":280},"obj":"Var"},{"id":"T4","span":{"begin":284,"end":290},"obj":"Gene"},{"id":"T5","span":{"begin":291,"end":300},"obj":"PosReg"},{"id":"T6","span":{"begin":305,"end":353},"obj":"MPA"},{"id":"T7","span":{"begin":358,"end":371},"obj":"NegReg"},{"id":"T8","span":{"begin":376,"end":420},"obj":"MPA"},{"id":"T12","span":{"begin":685,"end":694},"obj":"MPA"},{"id":"T9","span":{"begin":739,"end":748},"obj":"PosReg"},{"id":"T10","span":{"begin":756,"end":762},"obj":"Gene"},{"id":"T11","span":{"begin":763,"end":769},"obj":"Var"},{"id":"T13","span":{"begin":910,"end":916},"obj":"Gene"},{"id":"T14","span":{"begin":917,"end":925},"obj":"Var"},{"id":"T15","span":{"begin":930,"end":940},"obj":"Interaction"},{"id":"T16","span":{"begin":946,"end":952},"obj":"Gene"},{"id":"T17","span":{"begin":953,"end":960},"obj":"Var"},{"id":"T18","span":{"begin":993,"end":997},"obj":"PosReg"},{"id":"T19","span":{"begin":998,"end":1024},"obj":"MPA"}],"relations":[{"id":"R1","pred":"CauseOf","subj":"T3","obj":"T2"},{"id":"R10","pred":"ThemeOf","subj":"T13","obj":"T14"},{"id":"R11","pred":"ThemeOf","subj":"T14","obj":"T15"},{"id":"R12","pred":"ThemeOf","subj":"T17","obj":"T15"},{"id":"R13","pred":"ThemeOf","subj":"T16","obj":"T17"},{"id":"R14","pred":"CauseOf","subj":"T16","obj":"T15"},{"id":"R15","pred":"CauseOf","subj":"T17","obj":"T18"},{"id":"R16","pred":"ThemeOf","subj":"T19","obj":"T18"},{"id":"R2","pred":"ThemeOf","subj":"T4","obj":"T3"},{"id":"R3","pred":"CauseOf","subj":"T3","obj":"T5"},{"id":"R4","pred":"ThemeOf","subj":"T6","obj":"T5"},{"id":"R5","pred":"CauseOf","subj":"T3","obj":"T7"},{"id":"R6","pred":"ThemeOf","subj":"T8","obj":"T7"},{"id":"R7","pred":"ThemeOf","subj":"T10","obj":"T11"},{"id":"R8","pred":"CauseOf","subj":"T11","obj":"T9"},{"id":"R9","pred":"ThemeOf","subj":"T12","obj":"T9"}],"text":"POSITIVE REGULATOR OF IRON HOMEOSTASIS 1 (OsPRI1) positively regulates iron homeostasis in rice.\nOsHRZ1 is a potential iron-binding sensor. However, it is unclear how OsHRZ1 transmits signals. In this study, we reveal that OsPRI1 interacts with OsHRZ1. A loss-of-function mutation to OsPRI1 increased the sensitivity of plants to Fe-deficient conditions and downregulated the expression of Fe-deficiency-responsive genes. Yeast one-hybrid and electrophoretic mobility shift assay results suggested that OsPRI1 binds to the OsIRO2 and OsIRO3 promoters. In vitro ubiquitination experiments indicated that OsPRI1 is ubiquitinated by OsHRZ1. Cell-free degradation assays revealed that the stability of OsPRI1 decreased in wild type roots, but increased in the hrz1-2 mutant, suggesting OsHRZ1 is responsible for the instability of OsPRI1. The hrz1-2 seedlings were insensitive to Fe-deficient conditions. When the pri1-1 mutation was introduced into hrz1-2 mutants, the pri1hrz1 double mutant was more sensitive to Fe deficiency than the hrz1-2 mutant. Additionally, the expression levels of Fe-deficiency-responsive genes were lower in the hrz1pri1 double mutant than in the hrz1-2 mutant. Collectively, these results imply that OsPRI1, which is ubiquitinated by OsHRZ1, mediates rice responses to Fe-deficiency by positively regulating OsIRO2 and OsIRO3 expression as part of the OsHRZ1-OsPRI1-OsIRO2/3 signal transduction cascade."}
OryzaGP
{"project":"OryzaGP","denotations":[{"id":"T1","span":{"begin":97,"end":103},"obj":"gene"},{"id":"T2","span":{"begin":167,"end":173},"obj":"gene"},{"id":"T3","span":{"begin":223,"end":229},"obj":"gene"},{"id":"T4","span":{"begin":245,"end":251},"obj":"gene"},{"id":"T5","span":{"begin":284,"end":290},"obj":"gene"},{"id":"T6","span":{"begin":503,"end":509},"obj":"gene"},{"id":"T7","span":{"begin":523,"end":529},"obj":"gene"},{"id":"T8","span":{"begin":534,"end":540},"obj":"gene"},{"id":"T9","span":{"begin":603,"end":609},"obj":"gene"},{"id":"T10","span":{"begin":630,"end":636},"obj":"gene"},{"id":"T11","span":{"begin":698,"end":704},"obj":"gene"},{"id":"T12","span":{"begin":782,"end":788},"obj":"gene"},{"id":"T13","span":{"begin":827,"end":833},"obj":"gene"},{"id":"T14","span":{"begin":1226,"end":1232},"obj":"gene"},{"id":"T15","span":{"begin":1260,"end":1266},"obj":"gene"},{"id":"T16","span":{"begin":1334,"end":1340},"obj":"gene"},{"id":"T17","span":{"begin":1345,"end":1351},"obj":"gene"},{"id":"T18","span":{"begin":1378,"end":1384},"obj":"gene"},{"id":"T19","span":{"begin":1385,"end":1391},"obj":"gene"},{"id":"T20","span":{"begin":1392,"end":1400},"obj":"gene"}],"text":"POSITIVE REGULATOR OF IRON HOMEOSTASIS 1 (OsPRI1) positively regulates iron homeostasis in rice.\nOsHRZ1 is a potential iron-binding sensor. However, it is unclear how OsHRZ1 transmits signals. In this study, we reveal that OsPRI1 interacts with OsHRZ1. A loss-of-function mutation to OsPRI1 increased the sensitivity of plants to Fe-deficient conditions and downregulated the expression of Fe-deficiency-responsive genes. Yeast one-hybrid and electrophoretic mobility shift assay results suggested that OsPRI1 binds to the OsIRO2 and OsIRO3 promoters. In vitro ubiquitination experiments indicated that OsPRI1 is ubiquitinated by OsHRZ1. Cell-free degradation assays revealed that the stability of OsPRI1 decreased in wild type roots, but increased in the hrz1-2 mutant, suggesting OsHRZ1 is responsible for the instability of OsPRI1. The hrz1-2 seedlings were insensitive to Fe-deficient conditions. When the pri1-1 mutation was introduced into hrz1-2 mutants, the pri1hrz1 double mutant was more sensitive to Fe deficiency than the hrz1-2 mutant. Additionally, the expression levels of Fe-deficiency-responsive genes were lower in the hrz1pri1 double mutant than in the hrz1-2 mutant. Collectively, these results imply that OsPRI1, which is ubiquitinated by OsHRZ1, mediates rice responses to Fe-deficiency by positively regulating OsIRO2 and OsIRO3 expression as part of the OsHRZ1-OsPRI1-OsIRO2/3 signal transduction cascade."}