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Pesquisa : D08.811.277.656.262.500.792 [Categoria DeCS]
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[PMID]:28859055
[Au] Autor:Gurvits N; Löyttyniemi E; Nykänen M; Kuopio T; Kronqvist P; Talvinen K
[Ad] Endereço:Institute of Biomedicine, Department of Pathology and Forensic Medicine, University of Turku and Turku University Hospital, Turku 20510, Finland.
[Ti] Título:Separase is a marker for prognosis and mitotic activity in breast cancer.
[So] Source:Br J Cancer;117(9):1383-1391, 2017 Oct 24.
[Is] ISSN:1532-1827
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Cancer cell proliferation is a critical feature in classifying and predicting the outcome of breast carcinoma. Separase has a central role in cell cycle progression in unleashing sister-chromatids at anaphase onset. Abnormally functioning separase is known to lead to chromosomal instability. METHODS: The study comprises 349 breast carcinoma patients treated in Central Hospital of Central Finland. The prognostic value, role as a proliferation marker and regulatory interactions of separase are evaluated by immunohistochemical and double- and triple-immunofluorescence (IF) detections based on complete clinical data and >22-year follow-up of the patient material. RESULTS: In our material, abnormal separase expression predicted doubled risk of breast cancer death (P<0.001). Up to 11.3-year survival difference was observed when comparing patients with and without separase expressing cancer cell mitoses. Particularly, abnormal separase expression predicted impaired survival for luminal breast carcinoma (P<0.001, respectively). In multivariate analyses, abnormal separase expression showed independent prognostic value. The complex inhibitory interactions involving securin and cyclin B1 were investigated in double- and triple-IFs and revealed patient subgroups with aberrant regulation and expression patterns of separase. CONCLUSIONS: In our experience, separase is a promising and clinically applicable proliferation marker. Separase expression shows strong and independent prognostic value and could be developed into a biomarker for treatment decisions in breast carcinoma, particularly defining prognostic subgroups among luminal carcinomas.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/metabolismo
Neoplasias da Mama/patologia
Mitose/fisiologia
Securina/metabolismo
Separase/metabolismo
[Mh] Termos MeSH secundário: Neoplasias da Mama/metabolismo
Neoplasias da Mama/terapia
Feminino
Seres Humanos
Estadiamento de Neoplasias
Prognóstico
Taxa de Sobrevida
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Securin); EC 3.4.22.49 (Separase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170901
[St] Status:MEDLINE
[do] DOI:10.1038/bjc.2017.301


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[PMID]:28634715
[Au] Autor:Yao S; Guo Y; Dong SS; Hao RH; Chen XF; Chen YX; Chen JB; Tian Q; Deng HW; Yang TL
[Ad] Endereço:Key Laboratory of Biomedical Information Engineering of Ministry of Education, School of Life Science and Technology, Xi'an Jiaotong University, Xi'an, Shaanxi, 710049, People's Republic of China.
[Ti] Título:Regulatory element-based prediction identifies new susceptibility regulatory variants for osteoporosis.
[So] Source:Hum Genet;136(8):963-974, 2017 Aug.
[Is] ISSN:1432-1203
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Despite genome-wide association studies (GWASs) have identified many susceptibility genes for osteoporosis, it still leaves a large part of missing heritability to be discovered. Integrating regulatory information and GWASs could offer new insights into the biological link between the susceptibility SNPs and osteoporosis. We generated five machine learning classifiers with osteoporosis-associated variants and regulatory features data. We gained the optimal classifier and predicted genome-wide SNPs to discover susceptibility regulatory variants. We further utilized Genetic Factors for Osteoporosis Consortium (GEFOS) and three in-house GWASs samples to validate the associations for predicted positive SNPs. The random forest classifier performed best among all machine learning methods with the F1 score of 0.8871. Using the optimized model, we predicted 37,584 candidate SNPs for osteoporosis. According to the meta-analysis results, a list of regulatory variants was significantly associated with osteoporosis after multiple testing corrections and contributed to the expression of known osteoporosis-associated protein-coding genes. In summary, combining GWASs and regulatory elements through machine learning could provide additional information for understanding the mechanism of osteoporosis. The regulatory variants we predicted will provide novel targets for etiology research and treatment of osteoporosis.
[Mh] Termos MeSH primário: Osteoporose/genética
Polimorfismo de Nucleotídeo Único
Sequências Reguladoras de Ácido Nucleico
[Mh] Termos MeSH secundário: Algoritmos
Linhagem Celular
Galanina/genética
Galanina/metabolismo
Frequência do Gene
Predisposição Genética para Doença
Estudo de Associação Genômica Ampla
Seres Humanos
Modelos Genéticos
Reprodutibilidade dos Testes
Sensibilidade e Especificidade
Separase/genética
Separase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GAL protein, human); 88813-36-9 (Galanin); EC 3.4.22.49 (ESPL1 protein, human); EC 3.4.22.49 (Separase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.1007/s00439-017-1825-4


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[PMID]:28384135
[Au] Autor:Singleton MR; Uhlmann F
[Ad] Endereço:Structural Biology of Chromosome Segregation Laboratory, The Francis Crick Institute, London, UK.
[Ti] Título:Separase-securin complex: a cunning way to control chromosome segregation.
[So] Source:Nat Struct Mol Biol;24(4):337-339, 2017 04 06.
[Is] ISSN:1545-9985
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Segregação de Cromossomos
Securina/química
Securina/metabolismo
Separase/química
Separase/metabolismo
[Mh] Termos MeSH secundário: Animais
Cristalografia por Raios X
Seres Humanos
Modelos Moleculares
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Securin); EC 3.4.22.49 (Separase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170407
[St] Status:MEDLINE
[do] DOI:10.1038/nsmb.3393


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[PMID]:28263324
[Au] Autor:Boland A; Martin TG; Zhang Z; Yang J; Bai XC; Chang L; Scheres SH; Barford D
[Ad] Endereço:MRC Laboratory of Molecular Biology, Cambridge, UK.
[Ti] Título:Cryo-EM structure of a metazoan separase-securin complex at near-atomic resolution.
[So] Source:Nat Struct Mol Biol;24(4):414-418, 2017 Apr.
[Is] ISSN:1545-9985
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Separase is a caspase-family protease that initiates chromatid segregation by cleaving the kleisin subunits (Scc1 and Rec8) of cohesin, and regulates centrosome duplication and mitotic spindle function through cleavage of kendrin and Slk19. To understand the mechanisms of securin regulation of separase, we used single-particle cryo-electron microscopy (cryo-EM) to determine a near-atomic-resolution structure of the Caenorhabditis elegans separase-securin complex. Separase adopts a triangular-shaped bilobal architecture comprising an N-terminal tetratricopeptide repeat (TPR)-like α-solenoid domain docked onto the conserved C-terminal protease domain. Securin engages separase in an extended antiparallel conformation, interacting with both lobes. It inhibits separase by interacting with the catalytic site through a pseudosubstrate mechanism, thus revealing that in the inhibited separase-securin complex, the catalytic site adopts a conformation compatible with substrate binding. Securin is protected from cleavage because an aliphatic side chain at the P1 position represses protease activity by disrupting the organization of catalytic site residues.
[Mh] Termos MeSH primário: Microscopia Crioeletrônica
Securina/ultraestrutura
Separase/ultraestrutura
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Caenorhabditis elegans
Seres Humanos
Modelos Moleculares
Ligação Proteica
Domínios Proteicos
Estabilidade Proteica
Estrutura Secundária de Proteína
Securina/química
Separase/química
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Securin); EC 3.4.22.49 (Separase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170307
[St] Status:MEDLINE
[do] DOI:10.1038/nsmb.3386


  5 / 245 MEDLINE  
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[PMID]:28146474
[Au] Autor:Luo S; Tong L
[Ad] Endereço:Department of Biological Sciences, Columbia University, New York, New York 10027, USA.
[Ti] Título:Molecular mechanism for the regulation of yeast separase by securin.
[So] Source:Nature;542(7640):255-259, 2017 02 09.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Separase is a cysteine protease with a crucial role in the dissolution of cohesion among sister chromatids during chromosome segregation. In human tumours separase is overexpressed, making it a potential target for drug discovery. The protease activity of separase is strictly regulated by the inhibitor securin, which forms a tight complex with separase and may also stabilize this enzyme. Separases are large, 140-250-kilodalton enzymes, with an amino-terminal α-helical region and a carboxy-terminal caspase-like catalytic domain. Although crystal structures of the C-terminal two domains of separase and low-resolution electron microscopy reconstructions of the separase-securin complex have been reported, the atomic structures of full-length separase and especially the complex with securin are unknown. Here we report crystal structures at up to 2.6 Å resolution of the yeast Saccharomyces cerevisiae separase-securin complex. The α-helical region of separase (also known as Esp1) contains four domains (I-IV), and a substrate-binding domain immediately precedes the catalytic domain and has tight associations with it. The separase-securin complex assumes a highly elongated structure. Residues 258-373 of securin (Pds1), named the separase interaction segment, are primarily in an extended conformation and traverse the entire length of separase, interacting with all of its domains. Most importantly, residues 258-269 of securin are located in the separase active site, illuminating the mechanism of inhibition. Biochemical studies confirm the structural observations and indicate that contacts outside the separase active site are crucial for stabilizing the complex, thereby defining an important function for the helical region of separase.
[Mh] Termos MeSH primário: Proteínas de Saccharomyces cerevisiae/antagonistas & inibidores
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/química
Saccharomyces cerevisiae/enzimologia
Securina/química
Securina/metabolismo
Separase/antagonistas & inibidores
Separase/química
[Mh] Termos MeSH secundário: Domínio Catalítico
Cristalografia por Raios X
Estabilidade Enzimática
Modelos Moleculares
Ligação Proteica
Domínios Proteicos
Domínios e Motivos de Interação entre Proteínas
Separase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (PDS1 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Securin); EC 3.4.22.49 (ESP1 protein, S cerevisiae); EC 3.4.22.49 (Separase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170202
[St] Status:MEDLINE
[do] DOI:10.1038/nature21061


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[PMID]:28017619
[Au] Autor:Argüello-Miranda O; Zagoriy I; Mengoli V; Rojas J; Jonak K; Oz T; Graf P; Zachariae W
[Ad] Endereço:Laboratory of Chromosome Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
[Ti] Título:Casein Kinase 1 Coordinates Cohesin Cleavage, Gametogenesis, and Exit from M Phase in Meiosis II.
[So] Source:Dev Cell;40(1):37-52, 2017 Jan 09.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Meiosis consists of DNA replication followed by two consecutive nuclear divisions and gametogenesis or spore formation. While meiosis I has been studied extensively, less is known about the regulation of meiosis II. Here we show that Hrr25, the conserved casein kinase 1δ of budding yeast, links three mutually independent key processes of meiosis II. First, Hrr25 induces nuclear division by priming centromeric cohesin for cleavage by separase. Hrr25 simultaneously phosphorylates Rec8, the cleavable subunit of cohesin, and removes from centromeres the cohesin protector composed of shugoshin and the phosphatase PP2A. Second, Hrr25 initiates the sporulation program by inducing the synthesis of membranes that engulf the emerging nuclei at anaphase II. Third, Hrr25 mediates exit from meiosis II by activating pathways that trigger the destruction of M-phase-promoting kinases. Thus, Hrr25 synchronizes formation of the single-copy genome with gamete differentiation and termination of meiosis.
[Mh] Termos MeSH primário: Caseína Quinase I/metabolismo
Proteínas de Ciclo Celular/metabolismo
Proteínas Cromossômicas não Histona/metabolismo
Gametogênese
Meiose
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/citologia
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Anáfase
Núcleo Celular/metabolismo
Centrômero/metabolismo
Fosforilação
Proteína Fosfatase 2/metabolismo
Proteólise
Separase/metabolismo
Fuso Acromático/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Chromosomal Proteins, Non-Histone); 0 (Saccharomyces cerevisiae Proteins); 0 (cohesins); EC 2.7.11.1 (Casein Kinase I); EC 2.7.11.1 (HRR25 protein, S cerevisiae); EC 3.1.3.16 (Protein Phosphatase 2); EC 3.4.22.49 (Separase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170816
[Lr] Data última revisão:
170816
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161227
[St] Status:MEDLINE


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[PMID]:27450768
[Au] Autor:Azzopardi M; Farrugia G; Balzan R
[Ad] Endereço:Department of Physiology & Biochemistry, University of Malta, Msida MSD 2080, Malta; Centre for Molecular Medicine and Biobanking, University of Malta, Msida MSD 2080, Malta. Electronic address: maria.c.azzopardi.10@um.edu.mt.
[Ti] Título:Cell-cycle involvement in autophagy and apoptosis in yeast.
[So] Source:Mech Ageing Dev;161(Pt B):211-224, 2017 Jan.
[Is] ISSN:1872-6216
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Regulation of the cell cycle and apoptosis are two eukaryotic processes required to ensure maintenance of genomic integrity, especially in response to DNA damage. The ease with which yeast, amongst other eukaryotes, can switch from cellular proliferation to cell death may be the result of a common set of biochemical factors which play dual roles depending on the cell's physiological state. A wide variety of homologues are shared between different yeasts and metazoans and this conservation confirms their importance. This review gives an overview of key molecular players involved in yeast cell-cycle regulation, and those involved in mechanisms which are induced by cell-cycle dysregulation. One such mechanism is autophagy which, depending on the severity and type of DNA damage, may either contribute to the cell's survival or death. Cell-cycle dysregulation due to checkpoint deficiency leads to mitotic catastrophe which in turn leads to programmed cell death. Molecular players implicated in the yeast apoptotic pathway were shown to play important roles in the cell cycle. These include the metacaspase Yca1p, the caspase-like protein Esp1p, the cohesin subunit Mcd1p, as well as the inhibitor of apoptosis protein Bir1p. The roles of these molecular players are discussed.
[Mh] Termos MeSH primário: Apoptose/fisiologia
Autofagia/fisiologia
Ciclo Celular/fisiologia
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Caspases/genética
Caspases/metabolismo
Proteínas de Ciclo Celular/genética
Proteínas de Ciclo Celular/metabolismo
Proteínas Cromossômicas não Histona/genética
Proteínas Cromossômicas não Histona/metabolismo
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Separase/genética
Separase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Bir1 protein, S cerevisiae); 0 (Carrier Proteins); 0 (Cell Cycle Proteins); 0 (Chromosomal Proteins, Non-Histone); 0 (MCD1 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); EC 3.4.22.- (Caspases); EC 3.4.22.- (MCA1 protein, S cerevisiae); EC 3.4.22.49 (ESP1 protein, S cerevisiae); EC 3.4.22.49 (Separase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170810
[Lr] Data última revisão:
170810
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160725
[St] Status:MEDLINE


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[PMID]:27530289
[Au] Autor:Do HT; Zhang N; Pati D; Gilbertson SR
[Ad] Endereço:Department of Chemistry, University of Houston, Houston, TX 77204, United States.
[Ti] Título:Synthesis and activity of benzimidazole-1,3-dioxide inhibitors of separase.
[So] Source:Bioorg Med Chem Lett;26(18):4446-4450, 2016 09 15.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Due to the oncogenic activity of cohesin protease, separase in human cancer cells, modulation of separase enzymatic activity could constitute a new therapeutic strategy for targeting resistant, separase-overexpressing aneuploid tumors. Herein, we report the synthesis, structural information, and structure-activity relationship (SAR) of separase inhibitors based on modification of the lead molecule 2,2-dimethyl-5-nitro-2H-benzimidazole-1,3-dioxide, named Sepin-1, (1) identified from a high-throughput-screen. Replacement of -NO2 at C5 with other functional groups reduce the inhibitory activity in separase enzymatic assay. Substitution of the two methyl groups with other alkyl chains at the C2 moderately improves the effects on the inhibitory activity of those compounds. Modifications on 2H-benzimidazole-1,3-dioxide or the skeleton have variable effect on inhibition of separase enzymatic activity. Density-functional theory (DFT) calculations suggest there may be a correlation between the charges on the oxide moieties on these compounds and their activity in inhibiting separase enzyme.
[Mh] Termos MeSH primário: Benzimidazóis/síntese química
Benzimidazóis/farmacologia
Inibidores Enzimáticos/farmacologia
Separase/antagonistas & inibidores
[Mh] Termos MeSH secundário: Benzimidazóis/química
Inibidores Enzimáticos/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Benzimidazoles); 0 (Enzyme Inhibitors); EC 3.4.22.49 (Separase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171122
[Lr] Data última revisão:
171122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160818
[St] Status:MEDLINE


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[PMID]:27495871
[Au] Autor:Agircan FG; Hata S; Nussbaum-Krammer C; Atorino E; Schiebel E
[Ad] Endereço:Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany.
[Ti] Título:Proximity mapping of human separase by the BioID approach.
[So] Source:Biochem Biophys Res Commun;478(2):656-62, 2016 09 16.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Separase is a caspase-like cysteine protease that is best known for its essential role during the metaphase-to-anaphase transition when it cleaves the cohesin ring complex that keeps the sister chromatids together. Another important function of separase is to regulate the process of centriole separation, known as centriole disengagement, at the end of mitosis. We used proximity-dependent biotin identification (BioID) to expand our knowledge on the identity of separase's proximity interactors. We show that separase BioID labeled two domains at the mother centriole: an area underneath the centriolar appendages and another at the proximal end of the mother centriole. BioID analysis identified more than 200 proximity interactors of separase, one being the Alström Syndrome Protein 1 (ALMS1) at the base of centrioles. Other proximity interactors are the histone chaperons NAP1L1 and NAP1L4, which localize to the spindle poles during mitosis and the spindle assembly checkpoint proteins BUBR1, SKA1 and SKA3 that reside at kinetochores in early mitosis. Finally, we show that depletion of BUBR1 homolog from Caenorhabditis elegans delayed the recruitment of separase to mitotic chromosomes, and eventually anaphase onset.
[Mh] Termos MeSH primário: Anáfase
Bioensaio
Centríolos/metabolismo
Centrossomo/metabolismo
Metáfase
Separase/metabolismo
[Mh] Termos MeSH secundário: Animais
Biotina/química
Caenorhabditis elegans/genética
Caenorhabditis elegans/crescimento & desenvolvimento
Caenorhabditis elegans/metabolismo
Linhagem Celular Tumoral
Centríolos/ultraestrutura
Centrossomo/ultraestrutura
Proteínas Cromossômicas não Histona/genética
Proteínas Cromossômicas não Histona/metabolismo
Cromossomos/metabolismo
Cromossomos/ultraestrutura
Embrião não Mamífero
Expressão Gênica
Células HeLa
Seres Humanos
Proteínas Associadas aos Microtúbulos/genética
Proteínas Associadas aos Microtúbulos/metabolismo
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Proteína 1 de Modelagem do Nucleossomo/genética
Proteína 1 de Modelagem do Nucleossomo/metabolismo
Ligação Proteica
Proteínas Serina-Treonina Quinases/genética
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas/genética
Proteínas/metabolismo
Separase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ALMS1 protein, human); 0 (Chromosomal Proteins, Non-Histone); 0 (Microtubule-Associated Proteins); 0 (NAP1L1 protein, human); 0 (NAP1L4 protein, human); 0 (Nuclear Proteins); 0 (Nucleosome Assembly Protein 1); 0 (Proteins); 0 (SKA1 protein, human); 0 (Ska3 protein, human); 6SO6U10H04 (Biotin); EC 2.7.11.1 (BUB1 protein, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 3.4.22.49 (Separase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171127
[Lr] Data última revisão:
171127
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160807
[St] Status:MEDLINE


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[PMID]:27249343
[Au] Autor:Bachmann G; Richards MW; Winter A; Beuron F; Morris E; Bayliss R
[Ad] Endereço:Division of Structural Biology, The Institute of Cancer Research, London SW7 3RP, UK.
[Ti] Título:A closed conformation of the Caenorhabditis elegans separase-securin complex.
[So] Source:Open Biol;6(4):160032, 2016 Apr.
[Is] ISSN:2046-2441
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The protease separase plays a key role in sister chromatid disjunction and centriole disengagement. To maintain genomic stability, separase activity is strictly regulated by binding of an inhibitory protein, securin. Despite its central role in cell division, the separase and securin complex is poorly understood at the structural level. This is partly owing to the difficulty of generating a sufficient quantity of homogeneous, stable protein. Here, we report the production of Caenorhabditis elegans separase-securin complex, and its characterization using biochemical methods and by negative staining electron microscopy. Single particle analysis generated a density map at a resolution of 21-24 Å that reveals a close, globular structure of complex connectivity harbouring two lobes. One lobe matches closely a homology model of the N-terminal HEAT repeat domain of separase, whereas the second lobe readily accommodates homology models of the separase C-terminal death and caspase-like domains. The globular structure of the C. elegans separase-securin complex contrasts with the more elongated structure previously described for the Homo sapiens complex, which could represent a different functional state of the complex, suggesting a mechanism for the regulation of separase activity through conformational change.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/química
Caenorhabditis elegans/metabolismo
Complexos Multiproteicos/química
Securina/química
Separase/química
[Mh] Termos MeSH secundário: Animais
Proteínas de Caenorhabditis elegans/metabolismo
Proteínas de Caenorhabditis elegans/ultraestrutura
Biologia Computacional
Proteínas Intrinsicamente Desordenadas/química
Proteínas Intrinsicamente Desordenadas/metabolismo
Modelos Moleculares
Complexos Multiproteicos/metabolismo
Domínios Proteicos
Estabilidade Proteica
Securina/isolamento & purificação
Securina/metabolismo
Securina/ultraestrutura
Separase/isolamento & purificação
Separase/metabolismo
Separase/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Intrinsically Disordered Proteins); 0 (Multiprotein Complexes); 0 (Securin); EC 3.4.22.49 (Separase)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160602
[St] Status:MEDLINE



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