Structural insights into the transcriptional regulation of carbon/nitrogen metabolism homeostasis in Synechocystis
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- 英文论文题名：Structural insights into the transcriptional regulation of carbon/nitrogen metabolism homeostasis in Synechocystis
- 论文作者：Yong-Liang Jiang ; Xue-Ping Wang ; Hui Sun ; Dong-Dong Cao ; Wang Cheng ; Yuxing Chen ; Cong-Zhao Zhou
- 英文论文作者：Yong-Liang Jiang ; Xue-Ping Wang ; Hui Sun ; Dong-Dong Cao ; Wang Cheng ; Yuxing Chen ; Cong-Zhao Zhou ; School of Life Sciences ; University of Science and Technology of China
- 年：2016
- 作者机构：School of Life Sciences,University of Science and Technology of China;
- 英文论文关键词：transcriptional regulation ; crystal structure ; CO_2 concentrating mechanism ; nitrogen metabolism ; cyanobacteria
- 会议召开时间：2016-12-19
- 会议录名称：中国晶体学会第六届学术年会暨会员代表大会（大分子晶体学分会）论文摘要集
- 英文会议录名称：Abstracts of the 6th Annual Conference of Chinese Crystallographic Society
- 语种：英文
- 分类号：Q943.2
- 学会代码：ZGJY
- 会议名称：中国晶体学会第六届学术年会暨会员代表大会（大分子晶体学分会）
- 会议地点：中国广东广州
- 主办单位：中国晶体学会
- 学会名称：中国晶体学会
- 页数：1
- 文件大小：113k
- 原文格式：D
- 会议级别：全国
摘要
Cyanobacteria are capable of acclimating and growing under a wide range of ambient CO_2 concentrations,which is conducted by the CO2 concentrating mechanism(CCM).Two Lys R-type transcription regulators(LTTRs),Ccm R and Cmp R,and one Abr B family of transcriptional regulator Cy Abr B are involved in the regulation of CCM.As aglobal regulator of the CCM,Ccm R acts as repressor of several CCM related genes.Despite of extensive studies of the LTTR activators,little is known about the regulatory mechanism of LTTR repressors,due to the absence of the full-length structures.Here we found that 2-phosphoglycolate(2-PG) binds to Ccm R regulatory domain with a Kd value of 0.43 m M,which indicates that 2-PG might be an inducer of Ccm R.To find the structural insights into 2-PG regulated Ccm R transcription,we solved the full-length structure of Ccm R and the complex structure of the Ccm R regulatory domain with 2-PG.The full-length structure revealed that Ccm R has a tetrameric arrangement assembled via two distinct dimerization interfaces.Binding of 2-PG induces a significant conformational change of the Ccm R regulatory domain,which facilitates themovement of the DNA-binding domains.Consequently,the Ccm R tetramer alleviates the DNA-binding ability by relocation of the DNA-binding sites,which subsequently relieves the repressive effect of Ccm R and induces the transcription of target genes.Moreover,the DNA-binding affinity of Ccm R is significantly augmented in the presence of 2-oxoglutarate,which is a key metabolite that links the nitrogen and carbon metabolic pathways.Thus we propose that Ccm R might be a transcription factor that maintains the intracellular homeostasis of carbon/nitrogen.
Cyanobacteria are capable of acclimating and growing under a wide range of ambient CO_2 concentrations,which is conducted by the CO2 concentrating mechanism(CCM).Two Lys R-type transcription regulators(LTTRs),Ccm R and Cmp R,and one Abr B family of transcriptional regulator Cy Abr B are involved in the regulation of CCM.As aglobal regulator of the CCM,Ccm R acts as repressor of several CCM related genes.Despite of extensive studies of the LTTR activators,little is known about the regulatory mechanism of LTTR repressors,due to the absence of the full-length structures.Here we found that 2-phosphoglycolate(2-PG) binds to Ccm R regulatory domain with a Kd value of 0.43 m M,which indicates that 2-PG might be an inducer of Ccm R.To find the structural insights into 2-PG regulated Ccm R transcription,we solved the full-length structure of Ccm R and the complex structure of the Ccm R regulatory domain with 2-PG.The full-length structure revealed that Ccm R has a tetrameric arrangement assembled via two distinct dimerization interfaces.Binding of 2-PG induces a significant conformational change of the Ccm R regulatory domain,which facilitates themovement of the DNA-binding domains.Consequently,the Ccm R tetramer alleviates the DNA-binding ability by relocation of the DNA-binding sites,which subsequently relieves the repressive effect of Ccm R and induces the transcription of target genes.Moreover,the DNA-binding affinity of Ccm R is significantly augmented in the presence of 2-oxoglutarate,which is a key metabolite that links the nitrogen and carbon metabolic pathways.Thus we propose that Ccm R might be a transcription factor that maintains the intracellular homeostasis of carbon/nitrogen.
Cyanobacteria are capable of acclimating and growing under a wide range of ambient CO_2 concentrations,which is conducted by the CO2 concentrating mechanism(CCM).Two Lys R-type transcription regulators(LTTRs),Ccm R and Cmp R,and one Abr B family of transcriptional regulator Cy Abr B are involved in the regulation of CCM.As aglobal regulator of the CCM,Ccm R acts as repressor of several CCM related genes.Despite of extensive studies of the LTTR activators,little is known about the regulatory mechanism of LTTR repressors,due to the absence of the full-length structures.Here we found that 2-phosphoglycolate(2-PG) binds to Ccm R regulatory domain with a Kd value of 0.43 m M,which indicates that 2-PG might be an inducer of Ccm R.To find the structural insights into 2-PG regulated Ccm R transcription,we solved the full-length structure of Ccm R and the complex structure of the Ccm R regulatory domain with 2-PG.The full-length structure revealed that Ccm R has a tetrameric arrangement assembled via two distinct dimerization interfaces.Binding of 2-PG induces a significant conformational change of the Ccm R regulatory domain,which facilitates themovement of the DNA-binding domains.Consequently,the Ccm R tetramer alleviates the DNA-binding ability by relocation of the DNA-binding sites,which subsequently relieves the repressive effect of Ccm R and induces the transcription of target genes.Moreover,the DNA-binding affinity of Ccm R is significantly augmented in the presence of 2-oxoglutarate,which is a key metabolite that links the nitrogen and carbon metabolic pathways.Thus we propose that Ccm R might be a transcription factor that maintains the intracellular homeostasis of carbon/nitrogen.
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