检索结果-南通市图书馆

Molecular actions of NLR immune receptors in plants and animals

在线全文

学校读者我要写书评

暂无评论

Science China(Life Sciences) 2020年第9期63卷 1303-1316页

作者： Jizong Wang jijie chai Beijing Advanced Innovation Center for Structural Biology Tsinghua-Peking Joint Center for Life SciencesCenter for Plant BiologySchool of Life SciencesTsinghua UniversityBeijing 100084China Max-Planck Institute for Plant Breeding Research Cologne 50829Germany Institute of Biochemistry University of CologneCologne 50674Germany

NLRs constitute intracellular immune receptors in both plants and animals. Direct or indirect ligand recognition results in formation of oligomeric NLR complexes to mediate immune signaling. Over the past 20 years, rapid progress has been made in our understanding of NLR signaling. Structural and biochemical studies provide insight into molecular basis of autoinhibition,ligand recognition, and resistosome/inflammasome formation of several NLRs. In this review, we summarize these studies focusing on the structural aspect of NLRs. We also discuss the analogies and differences between plant and animal NLRs in their mechanisms of action and how the available knowledge may shed light on the signaling mechanisms of other NLRs.

关键词： NLR immune receptor autoihibition pathogen perception resistosome/inflammasome molecular mechanism

Door to the cell for COVID-19 opened,leading way to therapies

在线全文

学校读者我要写书评

暂无评论

Signal Transduction and Targeted Therapy 2020年第1期5卷 1514-1515页

作者： Zhiwei Huang jijie chai Center for Life Sciences School of Life Science and TechnologyHarbin Institute of TechnologyHarbin 150080China School of Life Sciences Tsinghua UniversityBeijing 100084China

A very recent study by Lan et al.1 published in Nature determined the crystal structure of the severe acute respiratory syndrome coronavirus(SARS-CoV)-2 receptor-binding domain(RBD)bound to angiotensin-converting enzyme 2(ACE2).The structure reveals the mechanism of SARS-CoV-2 RBD recognition by its receptor ACE2,which is highly conserved in ACE2 recognition of SARS-CoV *** study provides structural information on developing small molecules targeting SARS-CoV-2 RBD/ACE2 and implies the existence of other mechanisms than receptor binding for the markedly different infection activity of the two evolutionarily close viruses.

关键词： ACE2 markedly al

Apoptosome and inflammasome: conserved machineries for caspase activation

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

National Science Review 2014年第1期1卷 101-118页

作者： jijie chai Yigong Shi Center for Life Sciences School of Life Sciences and School of MedicineTsinghua University

Apoptosome and inlammasome are multimeric protein complexes that mediate the activation of speciic caspases at the onset of apoptosis and *** central component of apoptosome or inlammasome is a tripartite scafold protein,exempliied by Apaf-1 and NLRC4,which contains an amino-terminal homotypic interaction motif,a central nucleotide-binding oligomerization domain and a carboxyl-terminal ligand-sensing *** the absence of death cue or an inlammatory signal,Apaf-1 or NLRC4 exists in an auto-inhibited,monomeric state,which is stabilized by adenosine diphosphate(ADP).Binding to an apoptosis-or inlammation-inducing ligand,together with replacement of ADP by adenosine triphosphate(ATP),results in the formation of a multimeric apoptosome or *** assembled apoptosome and inlammasome serve as dedicated machineries to facilitate the activation of speciic *** this review,we describe the structure and functional mechanisms of mammalian inlammasome and apoptosomes from three representative *** is placed on the molecular mechanism of caspase activation and the shared features of apoptosomes and inlammasomes.

关键词： apoptosome inlammasome caspase activation apoptosis inlammation

Structure, biochemical function, and signaling mechanism of plant NLRs

在线全文

同方期刊数据库

学校读者我要写书评

暂无评论

Molecular Plant 2023年第1期16卷 75-95页

作者： Jizong Wang Wen Song jijie chai State Key Laboratory of Protein and Plant Gene Research School of Advanced Agricultural SciencesPeking UniversityBeijing 100871China Tsinghua-Peking Joint Center for Life Sciences Center for Plant BiologySchool of Life SciencesTsinghua UniversityBeijing 100084China Institute of Biochemistry University of Cologne50674 CologneGermany Max Planck Institute for Plant Breeding Research 50829 CologneGermany Peking University Institute of Advanced Agricultural Sciences Shandong Laboratory of Advanced Agricultural Sciences at WeifangWeifangShandong 261000China

To counter pathogen invasion,plants have evolved a large number of immune receptors,including membrane-resident pattern recognition receptors(PRRs)and intracellular nucleotide-binding and leucine-rich repeat receptors(NLRs).Our knowledge about PRR and NLR signaling mechanisms has expanded significantly over the past few *** NLRs form multi-protein complexes called resistosomes in response to pathogen effectors,and the signaling mediated by NLR resistosomes converges on Ca2+-permeable ***2+-permeable channels important for PRR signaling have also been *** findings highlight a crucial role of Ca2+in triggering plant immune *** this review,we first discuss the structural and biochemical mechanisms of non-canonical NLR Ca2+channels and then summarize our knowledge about immune-related Ca2+-permeable channels and their roles in PRR and NLR *** also discuss the potential role of Ca2+in the intricate interaction between PRR and NLR signaling.

关键词： plant immunity PRR NLR resistosome Ca2+-permeable channels Ca2+signaling second messenger

Structural basis for differential recognition of brassinolide by its receptors

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

Protein & Cell 2013年第6期4卷 475-482页

作者： Ji She Zhifu Han Bin Zhou jijie chai School of Life Sciences Peking UniversityBeijing 100871China National Institute of Biological Sciences Beijing 102206China School of Life Sciences Tsinghua UniversityBeijing 100084China College of Biological Sciences China Agricultural UniversityBeijing 100083China Tsinghua-Peking Center for Life Sciences Beijing 100084China

Brassinosteroids,a group of plant steroid hormones,reg-ulate many aspects of plant growth and *** and other have previously solved the crystal structures of BRI1(LRR)in complex with brassinolide,the most active brassinosteroid identifi ed thus *** these studies provide a structural basis for the recognition of brassi-nolide by its receptor BRI1,it still remains poorly under-stood how the hormone differentiates among its con-served *** we present the crystal structure of the BRI1 homolog BRL1 in complex with *** structure shows that subtle differences around the brassinolide binding site can generate a striking effect on its recognition by the BRI1 family of *** comparison of BRL1 and BRI1 in their brassinolide-bound forms reveals the molecular basis for differential binding of brassinolide to its different receptors,which can be used for more effi cient design of plant growth regulators for agricultural *** the basis of our structural studies and others’data,we also suggest possible mech-anisms for the activation of BRI1 family receptors.

关键词： X-ray crystallography leucine-rich repeat domain brassinosteroid BRL1

A loop matters for FTO substrate selection

在线全文

学校读者我要写书评

暂无评论

Protein & Cell 2010年第7期1卷 616-620页

作者： Zhifu Han Ning Huang Tianhui Niu jijie chai National Institute of Biological Sciences No.7 Science Park RoadBeijing 102206China College of Biological Sciences and Biotechnology Tsinghua UniversityBeijing 100084China

Recent studies have unequivocally established the link between FTO and *** was biochemically shown to belong to the AlkB-like family DNA/RNA ***,FTO differs from other AlkB members in that it has unique substrate specificity and contains an extended C-terminus with unknown *** into the substrate selection mechanism and a functional clue to the C-terminus of FTO were gained from recent structural and biochemical *** data would be valuable to design FTO-specific inhibitors that can be potentially translated into therapeutic agents for treatment of obesity or obesity-related diseases.

关键词： FTO gained specificity

Structural insight into chitin perception by chitin elicitor receptor kinase 1 of Oryza sativa

在线全文

学校读者我要写书评

暂无评论

Journal of Integrative Plant Biology 2023年第1期65卷 235-248页

作者： Li Xu Jizong Wang Yu Xiao Zhifu Han jijie chai Tsinghua-Peking Center for Life Sciences Beijing Advanced Innovation Center for Structural BiologyCentre for Plant Biology School of Life Sciences Tsinghua UniversityBeijing 100084 China Max Planck Institute for Plant Breeding Research Cologne 50829 Germany Institute of Biochemistry University of Cologne Cologne 50674 Germany Cluster of Excellence in Plant Sciences(CEPLAS) Düsseldorf 40225 Germany

Plants have developed innate immune systems to fight against pathogenic fungi by monitoring pathogenic signals known as pathogen-associated molecular patterns(PAMP)and have established endo symbiosis with arbuscular mycorrhizal(AM)fungi through recognition of mycorrhizal(Myc)*** elicitor receptor kinase 1 of Oryza sativa ***(OsC ERK1)plays a bifunctional role in mediating both chitin-triggered immunity and symbiotic relationships with AM ***,it remains unclear whether OsC ERK1 can directly recognize chitin *** this study,we show that OsC ERK1 binds to the chitin hexamer((NAG)6)and tetramer((NAG)4)directly and determine the crystal structure of the OsC ERK1-(NAG)6complex at 2?.The structure shows that one OsC ERK1 is associated with one(NAG)*** recognition,chitin hexamer binds OsC ERK1 by interacting with the shallow groove on the surface of LysM *** structural findings,complemented by mutational analyses,demonstrate that LysM 2 is crucial for recognition of both(NAG)6and(NAG)***,these findings provide structural insights into the ability of OsC ERK1 in chitin perception,which will lead to a better understanding of the role of OsCERK1 in mediating both immunity and symbiosis in rice.

关键词： chitin immune response OsCERK1 recognition mechanism symbiotic reaction

Crystal structure of a plant leucine rich repeat protein with two island domains

在线全文

学校读者我要写书评

暂无评论

Science China(Life Sciences) 2014年第1期57卷 137-144页

作者： SONG Wen HAN ZhiFu SUN YaDong chai jijie School of Life Sciences Tsinghua-Peking Center for Life Sciences Tsinghua University

Leucine rich repeat(LRR)domain,characterized by a repetitive sequence pattern rich in leucine residues,is a universal protein-protein interaction motif present in all life *** repeats interrupted by sequences of 30 70 residues(termed island domain,ID)have been found in some plant LRR receptor-like kinases(RLKs)and animal Toll-like receptors(TLR7-9).Recent studies provide insight into how a single ID is structurally integrated into an LRR ***,structural information on an LRR protein with two IDs is *** receptor-like protein kinase 2(RPK2)is an LRR-RLK and has important roles in controlling plant growth and development by perception and transduction of hormone *** we present the crystal structure of the extracellular LRR domain of RPK2(RPK2-LRR)containing two IDs from *** structure reveals that both of the IDs are helical and located at the central region of the single RPK2-LRR *** of them binds to the inner surface of the solenoid,whereas the other one mainly interacts with the lateral ***,a long loop immediately following the N-terminal capping domain of RPK2-LRR is presented toward and sandwiched between the two IDs,further stabilizing their embedding to the LRR solenoid.A potential ligand binding site formed by the two IDs and the solenoid is located at the C-terminal side of *** structural information of RPK2-LRR broadens our understanding toward the large family of LRR proteins and provides insight into RPK2-mediated signaling.

关键词： leucine rich repeat receptor-like kinases receptor-like protein kinase 2

Structural basis for a homodimeric ATPase subunit of an ECF transporter

在线全文

学校读者我要写书评

暂无评论

Protein & Cell 2013年第10期4卷 793-801页

作者： Chengliang chai You Yu Wei Zhuo Haifeng Zhao Xiaolu Li Na Wang jijie chai Maojun Yang College of Biological Sciences China Agricultural UniversityBeijing 100083China MOE Key Laboratory of Protein Sciences Tsinghua-Peking Center for Life SciencesSchool of Life SciencesTsinghua UniversityBeijing 100084China National Institute of Biological Sciences Beijing 102206China

The transition metal cobalt,an essential cofactor for many enzymes in prokaryotes,is taken up by several specifi c transport *** CbiMNQO protein complex be-longs to type-1 energy-coupling factor(ECF)transporters and is a widespread group of microbial cobalt *** is the ATPase subunit(A-component)of the cobalt transporting system in the gram-negative thermo-philic bacterium Thermoanaerobacter *** we report the crystal structure of a nucleotide-free CbiO at a resolution of 2.3Å.CbiO contains an N-terminal canonical nucleotide-binding domain(NBD)and C-termi-nal helical *** and biochemical data show that CbiO forms a homodimer mediated by the NBD and the C-terminal *** mainly via conserved hydrophobic amino acids between the two C-terminal do-mains result in formation of a four-helix *** comparison with other ECF transporters suggests that non-conserved residues outside the T-component bind-ing groove in the A component likely act as a specifi city determinant for T ***,our data provide information on understanding of the structural organiza-tion and interaction of the CbiMNQO system.

关键词： CbiO Cobalt ECF ATPase Thermoanaero-bacter tengcongensis