TOPLESS/TOPLESS-RELATED(TPL/TPR)proteins are transcriptional corepressors that play pivotal roles in plant development,hormone signaling,and stress responses.Although TPL/TPR proteins have been identified in various o...TOPLESS/TOPLESS-RELATED(TPL/TPR)proteins are transcriptional corepressors that play pivotal roles in plant development,hormone signaling,and stress responses.Although TPL/TPR proteins have been identified in various organisms,their functions in rice disease resistance remain largely unexplored.Here,we conducted a comprehensive analysis of the three rice TPL/TPR proteins,designated OsTPR1,OsTPR2,and OsTPR3,examining their evolutionary relationships,expression patterns,and subcellular localization,and assessing their roles in disease resistance.Phylogenetic analysis revealed that the three OsTPRs belonged to distinct evolutionary clades.Expression analysis demonstrated tissue-specific patterns and responsiveness to jasmonate(JA),with all three genes being induced upon infection with Xanthomonas oryzae pv.oryzae(Xoo).Consistent with their roles as transcriptional corepressors,all three OsTPRs localized to the nucleus.Disease resistance assays showed that,after inoculation with Xoo,lesion lengths on ostpr2 and ostpr3 mutants were significantly shorter than those on wild-type plants.Protein interaction assays demonstrated that OsTPR2 interacted with JA ZIM-domain protein(OsJAZ12),whose expression is also induced by Xoo.Furthermore,haplotype analysis of OsTPRs revealed natural variation,leading to the identification of superior allelic variants that confer improved resistance to bacterial blight without a yield penalty.Collectively,our findings provide a systematic characterization of TPL/TPR proteins in rice,highlight their potential roles in resistance to bacterial leaf blight,and identify valuable allelic resources for molecular breeding aimed at improving both disease resistance and yield.展开更多
Ethylene receptors play important roles not only in regulation of growth and development but also in response to environmental stimuli of plants. However, there are few reports on ethylene receptors in soybean. In thi...Ethylene receptors play important roles not only in regulation of growth and development but also in response to environmental stimuli of plants. However, there are few reports on ethylene receptors in soybean. In this article, putative ethylene receptors of soybean were searched from soybean genomic database （http：//www.phytozome.net/search.php） and analyzed. The ethylene receptor gene family in soybean comprising eight members, designated as GmERSI-1, GmERS1-2, GmETRI-1, GmETR1-2, GmETR2-1, GmETR2-2, GmEIN4-1, and GmEIN4-2 corresponding with their homologous genes in drabidopsis, were isolated and analyzed. Phylogenetic analysis indicated that the eight soybean ethylene receptors （SERs） were in two subfamilies and further divided into four groups, viz., groups I （GmERSI-1 and GmERS1-2）, 1I （GmETRI-1 and GmETR1-2）, VI （GmETR2-I and GmETR2-2）, and VII （GmEIN4-1 and GmEIN4-2）. Protein structure of the members in groups I and II from subfamily I were more conserved than the members in other two groups from subfamily II. Expression patterns of the SERs were compared with the homologous genes in Arabidopsis. The results demonstrated that expression patterns of the SERs differed from Arabidopsis members in the same group, suggesting that SERs are involved in different signal pathways compared to ethylene receptors in drabidopsis. Promoter analysis showed that the sequences of the members in each group were different from each other, and some specific binding elements of transcription factors detected in promoter sequences might explain the differences between the members in the same group. A novel soybean TPR protein （tetratricopeptide repeat protein）, GmTPR, was identified to interact with GmETRI-1, apparently an important ethylene receptor in ethylene signaling pathway in soybean. This suggested that GmTPR might be a novel downstream component of the ethylene signaling pathway.展开更多
Biogenesis of photosynthetic pigment/protein complexes is a highly regulated process that requires various assisting factors. Here, we report on the molecular analysis of the Pitt gene （sir1644） from the cyanobacter...Biogenesis of photosynthetic pigment/protein complexes is a highly regulated process that requires various assisting factors. Here, we report on the molecular analysis of the Pitt gene （sir1644） from the cyanobacterium Synechocystis sp. PCC 6803 （Synechocystis 6803） that encodes a membrane-bound tetratricopeptide repeat （TPR） protein of formerly unknown function. Targeted inactivation of Pitt affected photosynthetic performance and light-dependent chlorophyll synthesis. Yeast two-hybrid analyses and native PAGE strongly suggest a complex formation between Pitt and the light-dependent protochlorophyllide oxidoreductase （POR）. Consistently, POR levels are approximately threefold reduced in the pitt insertion mutant. The membrane sublocalization of Pitt was found to be dependent on the presence of the periplasmic photosystem Ⅱ （PSⅡ） biogenesis factor PratA, supporting the idea that Pitt is involved in the early steps of photosynthetic pigment/protein complex formation.展开更多
基金supported by the National Natural Science Foundation of China (Grant Nos. 32302291 and 32400207)the Zhejiang A&F University Research and Development Fund Project, China (Grant Nos. 2025LFR012 and 2022LFR127)
文摘TOPLESS/TOPLESS-RELATED(TPL/TPR)proteins are transcriptional corepressors that play pivotal roles in plant development,hormone signaling,and stress responses.Although TPL/TPR proteins have been identified in various organisms,their functions in rice disease resistance remain largely unexplored.Here,we conducted a comprehensive analysis of the three rice TPL/TPR proteins,designated OsTPR1,OsTPR2,and OsTPR3,examining their evolutionary relationships,expression patterns,and subcellular localization,and assessing their roles in disease resistance.Phylogenetic analysis revealed that the three OsTPRs belonged to distinct evolutionary clades.Expression analysis demonstrated tissue-specific patterns and responsiveness to jasmonate(JA),with all three genes being induced upon infection with Xanthomonas oryzae pv.oryzae(Xoo).Consistent with their roles as transcriptional corepressors,all three OsTPRs localized to the nucleus.Disease resistance assays showed that,after inoculation with Xoo,lesion lengths on ostpr2 and ostpr3 mutants were significantly shorter than those on wild-type plants.Protein interaction assays demonstrated that OsTPR2 interacted with JA ZIM-domain protein(OsJAZ12),whose expression is also induced by Xoo.Furthermore,haplotype analysis of OsTPRs revealed natural variation,leading to the identification of superior allelic variants that confer improved resistance to bacterial blight without a yield penalty.Collectively,our findings provide a systematic characterization of TPL/TPR proteins in rice,highlight their potential roles in resistance to bacterial leaf blight,and identify valuable allelic resources for molecular breeding aimed at improving both disease resistance and yield.
基金funded in part by the National Key Project for Research on Transgenic Biology (2011ZX08002-002 and 2011ZX08002-005)the National High-Tech R&D Program of China (2012AA10A309)
文摘Ethylene receptors play important roles not only in regulation of growth and development but also in response to environmental stimuli of plants. However, there are few reports on ethylene receptors in soybean. In this article, putative ethylene receptors of soybean were searched from soybean genomic database （http：//www.phytozome.net/search.php） and analyzed. The ethylene receptor gene family in soybean comprising eight members, designated as GmERSI-1, GmERS1-2, GmETRI-1, GmETR1-2, GmETR2-1, GmETR2-2, GmEIN4-1, and GmEIN4-2 corresponding with their homologous genes in drabidopsis, were isolated and analyzed. Phylogenetic analysis indicated that the eight soybean ethylene receptors （SERs） were in two subfamilies and further divided into four groups, viz., groups I （GmERSI-1 and GmERS1-2）, 1I （GmETRI-1 and GmETR1-2）, VI （GmETR2-I and GmETR2-2）, and VII （GmEIN4-1 and GmEIN4-2）. Protein structure of the members in groups I and II from subfamily I were more conserved than the members in other two groups from subfamily II. Expression patterns of the SERs were compared with the homologous genes in Arabidopsis. The results demonstrated that expression patterns of the SERs differed from Arabidopsis members in the same group, suggesting that SERs are involved in different signal pathways compared to ethylene receptors in drabidopsis. Promoter analysis showed that the sequences of the members in each group were different from each other, and some specific binding elements of transcription factors detected in promoter sequences might explain the differences between the members in the same group. A novel soybean TPR protein （tetratricopeptide repeat protein）, GmTPR, was identified to interact with GmETRI-1, apparently an important ethylene receptor in ethylene signaling pathway in soybean. This suggested that GmTPR might be a novel downstream component of the ethylene signaling pathway.
文摘Biogenesis of photosynthetic pigment/protein complexes is a highly regulated process that requires various assisting factors. Here, we report on the molecular analysis of the Pitt gene （sir1644） from the cyanobacterium Synechocystis sp. PCC 6803 （Synechocystis 6803） that encodes a membrane-bound tetratricopeptide repeat （TPR） protein of formerly unknown function. Targeted inactivation of Pitt affected photosynthetic performance and light-dependent chlorophyll synthesis. Yeast two-hybrid analyses and native PAGE strongly suggest a complex formation between Pitt and the light-dependent protochlorophyllide oxidoreductase （POR）. Consistently, POR levels are approximately threefold reduced in the pitt insertion mutant. The membrane sublocalization of Pitt was found to be dependent on the presence of the periplasmic photosystem Ⅱ （PSⅡ） biogenesis factor PratA, supporting the idea that Pitt is involved in the early steps of photosynthetic pigment/protein complex formation.
