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[PMID]:28740167
[Au] Autor:Soria-Bretones I; Cepeda-García C; Checa-Rodriguez C; Heyer V; Reina-San-Martin B; Soutoglou E; Huertas P
[Ad] Endereço:Departamento de Genética, Universidad de Sevilla, Sevilla, 41080, Spain.
[Ti] Título:DNA end resection requires constitutive sumoylation of CtIP by CBX4.
[So] Source:Nat Commun;8(1):113, 2017 07 24.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:DNA breaks are complex DNA lesions that can be repaired by two alternative mechanisms: non-homologous end-joining and homologous recombination. The decision between them depends on the activation of the DNA resection machinery, which blocks non-homologous end-joining and stimulates recombination. On the other hand, post-translational modifications play a critical role in DNA repair. We have found that the SUMO E3 ligase CBX4 controls resection through the key factor CtIP. Indeed, CBX4 depletion impairs CtIP constitutive sumoylation and DNA end processing. Importantly, mutating lysine 896 in CtIP recapitulates the CBX4-depletion phenotype, blocks homologous recombination and increases genomic instability. Artificial fusion of CtIP and SUMO suppresses the effects of both the non-sumoylatable CtIP mutant and CBX4 depletion. Mechanistically, CtIP sumoylation is essential for its recruitment to damaged DNA. In summary, sumoylation of CtIP at lysine 896 defines a subpopulation of the protein that is involved in DNA resection and recombination.The choice between non-homologous end-joining and homologous recombination to repair a DNA double-strand break depends on activation of the end resection machinery. Here the authors show that SUMO E3 ligase CBX4 sumoylates subpopulation of CtIP to regulate recruitment to breaks and resection.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Quebras de DNA de Cadeia Dupla
Reparo do DNA por Junção de Extremidades
Ligases/metabolismo
Proteínas Nucleares/metabolismo
Proteínas do Grupo Polycomb/metabolismo
[Mh] Termos MeSH secundário: Western Blotting
Proteínas de Transporte/genética
Linhagem Celular Tumoral
DNA/genética
DNA/metabolismo
Células HEK293
Recombinação Homóloga
Seres Humanos
Ligases/genética
Microscopia Confocal
Proteínas Nucleares/genética
Proteínas do Grupo Polycomb/genética
Interferência de RNA
Proteína SUMO-1/genética
Proteína SUMO-1/metabolismo
Proteínas Modificadoras Pequenas Relacionadas à Ubiquitina/genética
Proteínas Modificadoras Pequenas Relacionadas à Ubiquitina/metabolismo
Sumoilação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Nuclear Proteins); 0 (Polycomb-Group Proteins); 0 (RBBP8 protein, human); 0 (SUMO-1 Protein); 0 (SUMO1 protein, human); 0 (SUMO2 protein, human); 0 (Small Ubiquitin-Related Modifier Proteins); 9007-49-2 (DNA); EC 6.- (Ligases); EC 6.3.2.- (CBX4 protein, human)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-00183-6


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[PMID]:29045470
[Au] Autor:Surana P; Gowda CM; Tripathi V; Broday L; Das R
[Ad] Endereço:National Centre for Biological Sciences, Tata Institute of Fundamental Research, Bengaluru, India.
[Ti] Título:Structural and functional analysis of SMO-1, the SUMO homolog in Caenorhabditis elegans.
[So] Source:PLoS One;12(10):e0186622, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:SUMO proteins are important post-translational modifiers involved in multiple cellular pathways in eukaryotes, especially during the different developmental stages in multicellular organisms. The nematode C. elegans is a well known model system for studying metazoan development and has a single SUMO homolog, SMO-1. Interestingly, SMO-1 modification is linked to embryogenesis and development in the nematode. However, high-resolution information about SMO-1 and the mechanism of its conjugation is lacking. In this work, we report the high-resolution three dimensional structure of SMO-1 solved by NMR spectroscopy. SMO-1 has flexible N-terminal and C-terminal tails on either side of a rigid beta-grasp folded core. While the sequence of SMO-1 is more similar to SUMO1, the electrostatic surface features of SMO-1 resemble more with SUMO2/3. SMO-1 can bind to typical SUMO Interacting Motifs (SIMs). SMO-1 can also conjugate to a typical SUMOylation consensus site as well as to its natural substrate HMR-1. Poly-SMO-1 chains were observed in-vitro even though SMO-1 lacks any consensus SUMOylation site. Typical deSUMOylation enzymes like Senp2 can cleave the poly-SMO-1 chains. Despite being a single gene, the SMO-1 structure allows it to function in a large repertoire of signaling pathways involving SUMO in C. elegans. Structural and functional features of SMO-1 studies described here will be useful to understand its role in development.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/química
Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/metabolismo
Proteína SUMO-1/metabolismo
Homologia de Sequência de Aminoácidos
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Caderinas/metabolismo
Espectroscopia de Ressonância Magnética
Modelos Moleculares
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteína SUMO-1/química
Soluções
Eletricidade Estática
Sumoilação
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cadherins); 0 (Caenorhabditis elegans Proteins); 0 (SUMO-1 Protein); 0 (Solutions)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171019
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186622


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[PMID]:28768860
[Au] Autor:Chen SC; Jeng KS; Lai MMC
[Ad] Endereço:Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
[Ti] Título:Zinc Finger-Containing Cellular Transcription Corepressor ZBTB25 Promotes Influenza Virus RNA Transcription and Is a Target for Zinc Ejector Drugs.
[So] Source:J Virol;91(20), 2017 Oct 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Influenza A virus (IAV) replication relies on an intricate interaction between virus and host cells. How the cellular proteins are usurped for IAV replication remains largely obscure. The aim of this study was to search for novel and potential cellular factors that participate in IAV replication. ZBTB25, a transcription repressor of a variety of cellular genes, was identified by an RNA interference (RNAi) genomic library screen. Depletion of ZBTB25 significantly reduced IAV production. Conversely, overexpression of ZBTB25 enhanced it. ZBTB25 interacted with the viral RNA-dependent RNA polymerase (RdRp) protein and modulated its transcription activity. In addition, ZBTB25 also functioned as a viral RNA (vRNA)-binding protein, binding preferentially to the U-rich sequence within the 5' untranslated region (UTR) of vRNA. Both protein-protein and protein-RNA interactions involving ZBTB25 facilitated viral RNA transcription and replication. In addition, ZBTB25 suppressed interferon production, further enhancing viral replication. ZBTB25-associated functions required an intact zinc finger domain and posttranslational SUMO-1 modification of ZBTB25. Furthermore, treatment with disulfiram (a zinc ejector) of ZBTB25-overexpressing cells showed significantly reduced IAV production as a result of reduced RNA synthesis. Our findings indicate that IAV usurps ZBTB25 for IAV RNA synthesis and serves as a novel and potential therapeutic antiviral target. IAV-induced seasonal influenza causes severe illness and death in high-risk populations. However, IAV has developed resistance to current antiviral drugs due to its high mutation rate. Therefore, development of drugs targeting cellular factors required for IAV replication is an attractive alternative for IAV therapy. Here, we discovered a cellular protein, ZBTB25, that enhances viral RdRp activity by binding to both viral RdRp and viral RNA to stimulate viral RNA synthesis. A unique feature of ZBTB25 in the regulation of viral replication is its dual transcription functions, namely, promoting viral RNA transcription through binding to the U-rich region of vRNA and suppressing cellular interferon production. ZBTB25 contains a zinc finger domain that is required for RNA-inhibitory activity by chelating zinc ions. Disulfiram treatment disrupts the zinc finger functions, effectively repressing IAV replication. Based on our findings, we demonstrate that ZBTB25 regulates IAV RNA transcription and replication and serves as a promising antiviral target for IAV treatment.
[Mh] Termos MeSH primário: Proteínas de Ligação a DNA/metabolismo
Interações Hospedeiro-Patógeno
Vírus da Influenza A/genética
Proteínas Nucleares/metabolismo
Transcrição Genética
Zinco/metabolismo
[Mh] Termos MeSH secundário: Células A549
Antivirais/farmacologia
Proteínas de Ligação a DNA/deficiência
Proteínas de Ligação a DNA/genética
Dissulfiram/farmacologia
Células HEK293
Seres Humanos
Vírus da Influenza A/efeitos dos fármacos
Vírus da Influenza A/enzimologia
Vírus da Influenza A/fisiologia
Proteínas Nucleares/deficiência
Proteínas Nucleares/genética
Ligação Proteica
RNA Replicase/metabolismo
RNA Viral/metabolismo
Proteína SUMO-1/metabolismo
Replicação Viral/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (DNA-Binding Proteins); 0 (Nuclear Proteins); 0 (RNA, Viral); 0 (SUMO-1 Protein); 137951-89-4 (ZBTB25 protein, human); EC 2.7.7.48 (RNA Replicase); J41CSQ7QDS (Zinc); TR3MLJ1UAI (Disulfiram)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170804
[St] Status:MEDLINE


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[PMID]:28734548
[Au] Autor:Wang Z; Zhu WG; Xu X
[Ad] Endereço:Guangdong Key Laboratory of Genome Stability & Disease Prevention, Shenzhen University School of Medicine, Shenzhen, Guangdong 518060, China.
[Ti] Título:Ubiquitin-like modifications in the DNA damage response.
[So] Source:Mutat Res;803-805:56-75, 2017 Oct.
[Is] ISSN:1873-135X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Genomic DNA is damaged at an extremely high frequency by both endogenous and environmental factors. An improper response to DNA damage can lead to genome instability, accelerate the aging process and ultimately cause various human diseases, including cancers and neurodegenerative disorders. The mechanisms that underlie the cellular DNA damage response (DDR) are complex and are regulated at many levels, including at the level of post-translational modification (PTM). Since the discovery of ubiquitin in 1975 and ubiquitylation as a form of PTM in the early 1980s, a number of ubiquitin-like modifiers (UBLs) have been identified, including small ubiquitin-like modifiers (SUMOs), neural precursor cell expressed, developmentally down-regulated 8 (NEDD8), interferon-stimulated gene 15 (ISG15), human leukocyte antigen (HLA)-F adjacent transcript 10 (FAT10), ubiquitin-fold modifier 1 (UFRM1), URM1 ubiquitin-related modifier-1 (URM1), autophagy-related protein 12 (ATG12), autophagy-related protein 8 (ATG8), fan ubiquitin-like protein 1 (FUB1) and histone mono-ubiquitylation 1 (HUB1). All of these modifiers have known roles in the cellular response to various forms of stress, and delineating their underlying molecular mechanisms and functions is fundamental in enhancing our understanding of human disease and longevity. To date, however, the molecular mechanisms and functions of these UBLs in the DDR remain largely unknown. This review summarizes the current status of PTMs by UBLs in the DDR and their implication in cancer diagnosis, therapy and drug discovery.
[Mh] Termos MeSH primário: Dano ao DNA
Ubiquitinação
[Mh] Termos MeSH secundário: Proteína 12 Relacionada à Autofagia/genética
Proteína 12 Relacionada à Autofagia/metabolismo
Proteínas Relacionadas à Autofagia/genética
Proteínas Relacionadas à Autofagia/metabolismo
Citocinas/genética
Citocinas/metabolismo
Regulação para Baixo
Descoberta de Drogas
Seres Humanos
Proteína NEDD8
Neoplasias/tratamento farmacológico
Neoplasias/genética
Processamento de Proteína Pós-Traducional
Proteínas/genética
Proteínas/metabolismo
Proteína SUMO-1/genética
Proteína SUMO-1/metabolismo
Ubiquitinas/genética
Ubiquitinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (ATG12 protein, human); 0 (Autophagy-Related Protein 12); 0 (Autophagy-Related Proteins); 0 (Cytokines); 0 (NEDD8 Protein); 0 (NEDD8 protein, human); 0 (Proteins); 0 (SUMO-1 Protein); 0 (UBD protein, human); 0 (UFM1 protein, human); 0 (Ubiquitins); 0 (Urm1 protein, human); 60267-61-0 (ISG15 protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170724
[St] Status:MEDLINE


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[PMID]:28582471
[Au] Autor:Brun S; Abella N; Berciano MT; Tapia O; Jaumot M; Freire R; Lafarga M; Agell N
[Ad] Endereço:Departament Biomedicina, Universitat de Barcelona, IDIBAPS, Barcelona, Spain.
[Ti] Título:SUMO regulates p21Cip1 intracellular distribution and with p21Cip1 facilitates multiprotein complex formation in the nucleolus upon DNA damage.
[So] Source:PLoS One;12(6):e0178925, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We previously showed that p21Cip1 transits through the nucleolus on its way from the nucleus to the cytoplasm and that DNA damage inhibits this transit and induces the formation of p21Cip1-containing intranucleolar bodies (INoBs). Here, we demonstrate that these INoBs also contain SUMO-1 and UBC9, the E2 SUMO-conjugating enzyme. Furthermore, whereas wild type SUMO-1 localized in INoBs, a SUMO-1 mutant, which is unable to conjugate with proteins, does not, suggesting the presence of SUMOylated proteins at INoBs. Moreover, depletion of the SUMO-conjugating enzyme UBC9 or the sumo hydrolase SENP2 changed p21Cip1 intracellular distribution. In addition to SUMO-1 and p21Cip1, cell cycle regulators and DNA damage checkpoint proteins, including Cdk2, Cyclin E, PCNA, p53 and Mdm2, and PML were also detected in INoBs. Importantly, depletion of UBC9 or p21Cip1 impacted INoB biogenesis and the nucleolar accumulation of the cell cycle regulators and DNA damage checkpoint proteins following DNA damage. The impact of p21Cip1 and SUMO-1 on the accumulation of proteins in INoBs extends also to CRM1, a nuclear exportin that is also important for protein translocation from the cytoplasm to the nucleolus. Thus, SUMO and p21Cip1 regulate the transit of proteins through the nucleolus, and that disruption of nucleolar export by DNA damage induces SUMO and p21Cip1 to act as hub proteins to form a multiprotein complex in the nucleolus.
[Mh] Termos MeSH primário: Nucléolo Celular/metabolismo
Inibidor de Quinase Dependente de Ciclina p21/genética
Regulação da Expressão Gênica
Organelas/metabolismo
Proteína SUMO-1/metabolismo
[Mh] Termos MeSH secundário: Nucléolo Celular/genética
Ciclina E/genética
Ciclina E/metabolismo
Quinase 2 Dependente de Ciclina/genética
Quinase 2 Dependente de Ciclina/metabolismo
Inibidor de Quinase Dependente de Ciclina p21/deficiência
Cisteína Endopeptidases/genética
Cisteína Endopeptidases/metabolismo
Dano ao DNA
Células HCT116
Seres Humanos
Carioferinas/genética
Carioferinas/metabolismo
Biogênese de Organelas
Organelas/genética
Antígeno Nuclear de Célula em Proliferação/genética
Antígeno Nuclear de Célula em Proliferação/metabolismo
Proteína da Leucemia Promielocítica/genética
Proteína da Leucemia Promielocítica/metabolismo
Ligação Proteica
Multimerização Proteica
Transporte Proteico
Proteínas Proto-Oncogênicas c-mdm2/genética
Proteínas Proto-Oncogênicas c-mdm2/metabolismo
Receptores Citoplasmáticos e Nucleares/genética
Receptores Citoplasmáticos e Nucleares/metabolismo
Proteína SUMO-1/genética
Transdução de Sinais
Proteína Supressora de Tumor p53/genética
Proteína Supressora de Tumor p53/metabolismo
Enzimas de Conjugação de Ubiquitina/deficiência
Enzimas de Conjugação de Ubiquitina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CDKN1A protein, human); 0 (Cyclin E); 0 (Cyclin-Dependent Kinase Inhibitor p21); 0 (Karyopherins); 0 (Proliferating Cell Nuclear Antigen); 0 (Promyelocytic Leukemia Protein); 0 (Receptors, Cytoplasmic and Nuclear); 0 (SUMO-1 Protein); 0 (SUMO1 protein, human); 0 (Tumor Suppressor Protein p53); 0 (exportin 1 protein); 143220-95-5 (PML protein, human); EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes); EC 2.3.2.27 (MDM2 protein, human); EC 2.3.2.27 (Proto-Oncogene Proteins c-mdm2); EC 2.7.11.22 (CDK2 protein, human); EC 2.7.11.22 (Cyclin-Dependent Kinase 2); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.- (SENP2 protein, human); EC 6.3.2.- (ubiquitin-conjugating enzyme UBC9)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170606
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0178925


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[PMID]:28575654
[Au] Autor:Dhingra N; Zhao X
[Ad] Endereço:Molecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
[Ti] Título:SUMO Teams Up with a Translocase to Save TOPO.
[So] Source:Mol Cell;66(5):577-578, 2017 Jun 01.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this issue of Molecular Cell, Wei et al. (2017) report how a DNA translocase uses SUMO as a cue to save Top2 from ubiquitin-mediated degradation and to minimize DNA breaks, thus providing insights into the SUMO and ubiquitin interplay in genome maintenance.
[Mh] Termos MeSH primário: Proteína SUMO-1/genética
Sumoilação
[Mh] Termos MeSH secundário: Seres Humanos
Compostos Organofosforados
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Organophosphorus Compounds); 0 (SUMO-1 Protein); 78-50-2 (trioctyl phosphine oxide)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170603
[St] Status:MEDLINE


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[PMID]:28572513
[Au] Autor:Lv Z; Yuan L; Atkison JH; Aldana-Masangkay G; Chen Y; Olsen SK
[Ad] Endereço:From the Department of Biochemistry and Molecular Biology and Hollings Cancer Center, Medical University of South Carolina, Charleston, South Carolina 29425 and.
[Ti] Título:Domain alternation and active site remodeling are conserved structural features of ubiquitin E1.
[So] Source:J Biol Chem;292(29):12089-12099, 2017 Jul 21.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:E1 enzymes for ubiquitin (Ub) and Ub-like modifiers (Ubls) harbor two catalytic activities that are required for Ub/Ubl activation: adenylation and thioester bond formation. Structural studies of the E1 for the Ubl mall biquitin-like difier (SUMO) revealed a single active site that is transformed by a conformational switch that toggles its competency for catalysis of these two distinct chemical reactions. Although the mechanisms of adenylation and thioester bond formation revealed by SUMO E1 structures are thought to be conserved in Ub E1, there is currently a lack of structural data supporting this hypothesis. Here, we present a structure of Uba1 in which the second catalytic cysteine half-domain (SCCH domain) harboring the catalytic cysteine has undergone a 106° rotation that results in a completely different network of intramolecular interactions between the SCCH and adenylation domains and translocation of the catalytic cysteine 12 Å closer to the Ub C terminus compared with previous Uba1 structures. SCCH domain alternation is accompanied by conformational changes within the Uba1 adenylation domains that effectively disassemble the adenylation active site. Importantly, the structural and biochemical data suggest that domain alternation and remodeling of the adenylation active site are interconnected and are intrinsic structural features of Uba1 and that the overall structural basis for adenylation and thioester bond formation exhibited by SUMO E1 is indeed conserved in Ub E1. Finally, the mechanistic insights provided by the novel conformational snapshot of Uba1 presented in this study may guide efforts to develop small molecule inhibitors of this critically important enzyme that is an active target for anticancer therapeutics.
[Mh] Termos MeSH primário: Modelos Moleculares
Processamento de Proteína Pós-Traducional
Proteína SUMO-1/metabolismo
Proteínas de Schizosaccharomyces pombe/metabolismo
Enzimas Ativadoras de Ubiquitina/metabolismo
Enzimas de Conjugação de Ubiquitina/metabolismo
Ubiquitina/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Domínio Catalítico
Cristalografia por Raios X
Cisteína/metabolismo
Bases de Dados de Proteínas
Dissulfetos/química
Dissulfetos/metabolismo
Dissulfetos/farmacologia
Ativação Enzimática
Inibidores Enzimáticos/química
Inibidores Enzimáticos/metabolismo
Inibidores Enzimáticos/farmacologia
Ligantes
Mutação
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica/efeitos dos fármacos
Processamento de Proteína Pós-Traducional/efeitos dos fármacos
Redobramento de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Proteína SUMO-1/química
Proteína SUMO-1/genética
Proteínas de Schizosaccharomyces pombe/antagonistas & inibidores
Proteínas de Schizosaccharomyces pombe/química
Proteínas de Schizosaccharomyces pombe/genética
Homologia Estrutural de Proteína
Ubiquitina/química
Ubiquitina/genética
Enzimas Ativadoras de Ubiquitina/antagonistas & inibidores
Enzimas Ativadoras de Ubiquitina/química
Enzimas Ativadoras de Ubiquitina/genética
Enzimas de Conjugação de Ubiquitina/química
Enzimas de Conjugação de Ubiquitina/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Disulfides); 0 (Enzyme Inhibitors); 0 (Ligands); 0 (NSC624206); 0 (Recombinant Proteins); 0 (SUMO-1 Protein); 0 (Schizosaccharomyces pombe Proteins); 0 (Ubiquitin); EC 2.3.2.23 (Ubc4 protein, S pombe); EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes); EC 6.2.1.45 (Ubiquitin-Activating Enzymes); EC 6.3.2.19 (ptr3 protein, S pombe); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170603
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.787622


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[PMID]:28532323
[Au] Autor:Takahashi D; Orihara Y; Kitagawa S; Kusakabe M; Shintani T; Oma Y; Harata M
[Ad] Endereço:a Laboratory of Molecular Biology, Graduate School of Agricultural Science , Tohoku University , Sendai , Japan.
[Ti] Título:Quantitative regulation of histone variant H2A.Z during cell cycle by ubiquitin proteasome system and SUMO-targeted ubiquitin ligases.
[So] Source:Biosci Biotechnol Biochem;81(8):1557-1560, 2017 Aug.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Quantitative control of histones and histone variants during cell cycle is relevant to their epigenetic functions. We found that the level of yeast histone variant H2A.Z in the G2/M-phase is actively kept low by the ubiquitin proteasome system and SUMO-targeted ubiquitin ligases. Overexpression of H2A.Z induced defects in mitotic progression, suggesting functional importance of this quantitative control.
[Mh] Termos MeSH primário: Regulação Fúngica da Expressão Gênica
Histonas/genética
Proteína SUMO-1/genética
Proteínas de Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/genética
Ubiquitina/genética
[Mh] Termos MeSH secundário: DNA Helicases/genética
DNA Helicases/metabolismo
Pontos de Checagem da Fase G2 do Ciclo Celular
Histonas/metabolismo
Mitose
Complexo de Endopeptidases do Proteassoma/metabolismo
Proteólise
Proteína SUMO-1/metabolismo
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Ubiquitina/metabolismo
Ubiquitina-Proteína Ligases/genética
Ubiquitina-Proteína Ligases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histones); 0 (Htz1 protein, S cerevisiae); 0 (SUMO-1 Protein); 0 (Saccharomyces cerevisiae Proteins); 0 (Ubiquitin); EC 2.3.2.27 (Slx8 protein, S cerevisiae); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 3.4.25.1 (Proteasome Endopeptidase Complex); EC 3.6.1.- (ULS1 protein, S cerevisiae); EC 3.6.4.- (DNA Helicases); EC 6.3.2.- (Slx5 protein, S cerevisiae)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170524
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1326087


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[PMID]:28342872
[Au] Autor:Wang J; Wen S; Zhao R; Qi J; Liu Z; Li W; An J; Wood C; Wang Y
[Ad] Endereço:TEDA Institute of Biological Sciences and Biotechnology, Nankai University, 23 Hongda Street, TEDA, Tianjin 300457, China; Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, 23 Hongda Street, TEDA, Tianjin 300457, China; Tianjin Key Laboratory of Microbial Functional Gen
[Ti] Título:Covalent conjugation of the equine infectious anemia virus Gag with SUMO.
[So] Source:Biochem Biophys Res Commun;486(3):712-719, 2017 May 06.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The conjugation of small ubiquitin-like modifier (SUMO) to the target protein, namely, SUMOylation, is involved in the regulation of many important biological events including host-pathogen interaction. Some viruses have evolved to exploit the host SUMOylation machinery to modify their own protein. Retroviral Gag protein plays critical roles in the viral life cycle. The HIV-1 p6 and the Moloney murine leukemia virus CA have been reported to be conjugated with SUMO. In this study, we report for the first time, to our knowledge, the covalent conjugation of equine infectious anemia virus (EIAV) Gag with SUMO. The C-terminal p9 domain of Gag is a main target for SUMOylation and SUMO is attached to multiple sites of p9, including K30 whose mutation abolished p9 SUMOylation completely. The SUMOylation of p9, but not the p9-K30 mutant, was also detected in equine fibroblastic cells ATCC CCL-57™. Ubc9 and its C93 residue are indispensable for the SUMOylation of p9. Using confocal microscopy, it is found that EIAV Gag localizes primarily, if not exclusively, in the cytoplasm of the cell and the co-localization of EIAV Gag with Ubc9 was observed. Our findings that EIAV Gag is SUMOylated at p9-K30, together with previous findings on the defects of p9-K30 mutant in viral DNA translocation from cytoplasm to the nucleus, suggests that SUMOylation of Gag may be involved in such functions.
[Mh] Termos MeSH primário: Produtos do Gene gag/genética
Vírus da Anemia Infecciosa Equina/genética
Lisina/metabolismo
Proteína SUMO-1/genética
Enzimas de Conjugação de Ubiquitina/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Linhagem Celular
Escherichia coli/genética
Escherichia coli/metabolismo
Fibroblastos/metabolismo
Fibroblastos/virologia
Regulação da Expressão Gênica
Produtos do Gene gag/metabolismo
Células HEK293
Cavalos
Interações Hospedeiro-Patógeno
Seres Humanos
Vírus da Anemia Infecciosa Equina/metabolismo
Mutação
Domínios Proteicos
Proteína SUMO-1/metabolismo
Transdução de Sinais
Sumoilação
Enzimas de Conjugação de Ubiquitina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gene Products, gag); 0 (SUMO-1 Protein); EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes); EC 6.3.2.- (ubiquitin-conjugating enzyme UBC9); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170602
[Lr] Data última revisão:
170602
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170327
[St] Status:MEDLINE


  10 / 1433 MEDLINE  
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[PMID]:28284030
[Au] Autor:Pichler A; Fatouros C; Lee H; Eisenhardt N
[Ti] Título:SUMO conjugation - a mechanistic view.
[So] Source:Biomol Concepts;8(1):13-36, 2017 Mar 01.
[Is] ISSN:1868-503X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The regulation of protein fate by modification with the small ubiquitin-related modifier (SUMO) plays an essential and crucial role in most cellular pathways. Sumoylation is highly dynamic due to the opposing activities of SUMO conjugation and SUMO deconjugation. SUMO conjugation is performed by the hierarchical action of E1, E2 and E3 enzymes, while its deconjugation involves SUMO-specific proteases. In this review, we summarize and compare the mechanistic principles of how SUMO gets conjugated to its substrate. We focus on the interplay of the E1, E2 and E3 enzymes and discuss how specificity could be achieved given the limited number of conjugating enzymes and the thousands of substrates.
[Mh] Termos MeSH primário: Sumoilação
[Mh] Termos MeSH secundário: Proteína SUMO-1/metabolismo
Especificidade por Substrato
Ubiquitina/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (SUMO-1 Protein); 0 (Ubiquitin); EC 2.3.2.27 (Ubiquitin-Protein Ligases)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170320
[Lr] Data última revisão:
170320
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170312
[St] Status:MEDLINE



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