The small ubiquitin-related modifier （SUMO） modification plays an important role in the regulation of abscisic acid （ABA） signaling, but the function of the SUMO protease, in ABA signaling, remains largely unknown...The small ubiquitin-related modifier （SUMO） modification plays an important role in the regulation of abscisic acid （ABA） signaling, but the function of the SUMO protease, in ABA signaling, remains largely unknown. Here, we show that the SUMO protease, ASPI positively regulates ABA signaling. Mutations in ASPI resulted in an ABA-insensitive phenotype, during early seedling develop- ment. Wild-type ASP1 successfully rescued, whereas an ASPI mutant （C577S）, defective in SUMO protease activity, failed to rescue, the ABA-insensitive phenotype of asp1-1. Expression of ABI5 and MYB3o target genes was attenuated in asp^-I and our genetic analyses revealed that ASP1 may function upstream of ABI5 and MYB3o.展开更多
目的：研究临床致病白念珠菌交配型基因MTL纯合子与杂合子的流行病学特点,分析其与外阴阴道念珠菌病患者的临床特征、白念珠菌致病力及毒力的关系。方法：通过普通PCR对临床外阴阴道念珠菌病患者阴道分泌物分离的致病白念珠菌MTL基因进...目的：研究临床致病白念珠菌交配型基因MTL纯合子与杂合子的流行病学特点,分析其与外阴阴道念珠菌病患者的临床特征、白念珠菌致病力及毒力的关系。方法：通过普通PCR对临床外阴阴道念珠菌病患者阴道分泌物分离的致病白念珠菌MTL基因进行检测,应用实时荧光定量PCR反应分析MTL纯合子与杂合子中毒力相关基因ASL3、SAP1和HWP1基因的表达,并采用Rosco药片扩散法对白念珠菌进行体外药物敏感试验。结果：1338株白念珠菌中,1330株为MTLa/α杂合子,8株为MTL纯合子（7株MTLa/a纯合子,1株MTLα/α纯合子）。8株MTL纯合子所致外阴阴道念珠菌病患者中6例患者达到真菌学治愈。与杂合子相比,白念珠菌MTL纯合子对唑类药物耐药性较高（0~75%vs 0~2.7%,P〈0.05）。毒力相关基因ASL3在两者中的表达无明显统计学差异,SAP1在MTL杂合子中表达稍高（1.02±0.68 vs 0.83±0.31,P〉0.05）,而HWP1在杂合子中表达明显增高（1.71±1.42 vs 1.20±0.62,P〈0.05）。结论：外阴阴道念珠菌病白念珠菌MTL纯合子在外阴阴道念珠菌病患者中流行率较低;与杂合子相比,MTL纯合子耐药性增加;而毒力相关基因HWP1、SAP1和ASL3在纯合子中表达降低,这与其临床特征相符。展开更多
In response to far-red light(FR),FAR-RED ELONGATED HYPOCOTYL 1(FHY1)transports the photoactivated phytochrome A(phyA),the primary FR photoreceptor,into the nucleus,where it initiates FR signaling in plants.Light promo...In response to far-red light(FR),FAR-RED ELONGATED HYPOCOTYL 1(FHY1)transports the photoactivated phytochrome A(phyA),the primary FR photoreceptor,into the nucleus,where it initiates FR signaling in plants.Light promotes the 26S proteasome-mediated degradation of FHY1,which desensitizes FR signaling,but the underlying regulatory mechanism remains largely unknown.Here,we show that reversible SUMOylation of FHY1 tightly regulates this process.Lysine K32(K32)and K103 are major SUMOylation sites of FHY1.We found that FR exposure promotes the SUMOylation of FHY1,which accelerates its degradation.Furthermore,we discovered that ARABIDOPSIS SUMO PROTEASE 1(ASP1)interacts with FHY1 in the nucleus under FR and facilitates its deSUMOylation.FHY1 was strongly SUMOylated and its protein level was decreased in the asp1-1 loss-of-function mutant compared with that in the wild type under FR.Consistently,asp1-1 seedlings exhibited a decreased sensitivity to FR,suggesting that ASP1 plays an important role in the maintenance of proper FHY1 levels under FR.Genetic analysis further revealed that ASP1 regulates FR signaling through an FHY1-and phyA-dependent pathway.Interestingly,We found that continuous FR inhibits ASP1 accumulation,perhaps contributing to the desensitization of FR signaling.Taken together,these results indicate that FR-induced SUMOylation and ASP1-dependent deSUMOylation of FHY1 represent a key regulatory mechanism that fine-tunes FR signaling.展开更多
基金supported by grants from the National Natural Science Foundation of China(31670186)the Chinese Academy of Sciences(XDA08010105)
文摘The small ubiquitin-related modifier （SUMO） modification plays an important role in the regulation of abscisic acid （ABA） signaling, but the function of the SUMO protease, in ABA signaling, remains largely unknown. Here, we show that the SUMO protease, ASPI positively regulates ABA signaling. Mutations in ASPI resulted in an ABA-insensitive phenotype, during early seedling develop- ment. Wild-type ASP1 successfully rescued, whereas an ASPI mutant （C577S）, defective in SUMO protease activity, failed to rescue, the ABA-insensitive phenotype of asp1-1. Expression of ABI5 and MYB3o target genes was attenuated in asp^-I and our genetic analyses revealed that ASP1 may function upstream of ABI5 and MYB3o.
文摘目的：研究临床致病白念珠菌交配型基因MTL纯合子与杂合子的流行病学特点,分析其与外阴阴道念珠菌病患者的临床特征、白念珠菌致病力及毒力的关系。方法：通过普通PCR对临床外阴阴道念珠菌病患者阴道分泌物分离的致病白念珠菌MTL基因进行检测,应用实时荧光定量PCR反应分析MTL纯合子与杂合子中毒力相关基因ASL3、SAP1和HWP1基因的表达,并采用Rosco药片扩散法对白念珠菌进行体外药物敏感试验。结果：1338株白念珠菌中,1330株为MTLa/α杂合子,8株为MTL纯合子（7株MTLa/a纯合子,1株MTLα/α纯合子）。8株MTL纯合子所致外阴阴道念珠菌病患者中6例患者达到真菌学治愈。与杂合子相比,白念珠菌MTL纯合子对唑类药物耐药性较高（0~75%vs 0~2.7%,P〈0.05）。毒力相关基因ASL3在两者中的表达无明显统计学差异,SAP1在MTL杂合子中表达稍高（1.02±0.68 vs 0.83±0.31,P〉0.05）,而HWP1在杂合子中表达明显增高（1.71±1.42 vs 1.20±0.62,P〈0.05）。结论：外阴阴道念珠菌病白念珠菌MTL纯合子在外阴阴道念珠菌病患者中流行率较低;与杂合子相比,MTL纯合子耐药性增加;而毒力相关基因HWP1、SAP1和ASL3在纯合子中表达降低,这与其临床特征相符。
基金This work was supported by the National Natural Science Foundation of China(grant nos.31670186 and 31870238)the Chinese Academy of Sciences(ZDRW-ZS-2019-2-0101,KFJ-STS-ZDTP-076-1,and The Innovative Academy of Seed Design).
文摘In response to far-red light(FR),FAR-RED ELONGATED HYPOCOTYL 1(FHY1)transports the photoactivated phytochrome A(phyA),the primary FR photoreceptor,into the nucleus,where it initiates FR signaling in plants.Light promotes the 26S proteasome-mediated degradation of FHY1,which desensitizes FR signaling,but the underlying regulatory mechanism remains largely unknown.Here,we show that reversible SUMOylation of FHY1 tightly regulates this process.Lysine K32(K32)and K103 are major SUMOylation sites of FHY1.We found that FR exposure promotes the SUMOylation of FHY1,which accelerates its degradation.Furthermore,we discovered that ARABIDOPSIS SUMO PROTEASE 1(ASP1)interacts with FHY1 in the nucleus under FR and facilitates its deSUMOylation.FHY1 was strongly SUMOylated and its protein level was decreased in the asp1-1 loss-of-function mutant compared with that in the wild type under FR.Consistently,asp1-1 seedlings exhibited a decreased sensitivity to FR,suggesting that ASP1 plays an important role in the maintenance of proper FHY1 levels under FR.Genetic analysis further revealed that ASP1 regulates FR signaling through an FHY1-and phyA-dependent pathway.Interestingly,We found that continuous FR inhibits ASP1 accumulation,perhaps contributing to the desensitization of FR signaling.Taken together,these results indicate that FR-induced SUMOylation and ASP1-dependent deSUMOylation of FHY1 represent a key regulatory mechanism that fine-tunes FR signaling.
