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[PMID]:29367487
[Au] Autor:Lin Y; Xie X; Yuan B; Fu J; Liu L; Tian H; Chen T; He D
[Ad] Endereço:College of Food Science and Engineering, Wuhan polytechnic University.
[Ti] Título:Optimization of Enzymatic Cell Disruption for Improving Lipid Extraction from Schizochytrium sp. through Response Surface Methodology.
[So] Source:J Oleo Sci;67(2):215-224, 2018 Feb 01.
[Is] ISSN:1347-3352
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:This study is aimed to explore the optimal conditions of cell disruption in the extraction algae oil process, using alkaline protease to disrupt cell of Schizochytrium sp. to extract oil in this paper. The effects of enzymatic lysis temperature, enzymatic lysis time, enzyme dosage and pH value on oil yield and DHA yield were studied. Through the combination of single factor test and response surface design, the optimal cell disruption conditions were screened out. The fatty acid composition of algal oil was analyzed by gas chromatography-massspectrometry (GC-MS). The results showed that when the conditions were: enzymatic lysis temperature 55°C, enzymatic lysis time 9 h, enzyme dosage 3% of biomass and pH 8,oil yield and DHA yield reached the highest 14.52 g/L and 7.12 g/L, respectively. When the strains were cultured in 50 L fermentor, oil yield reached 26.27 g/L and DHA yield reached 12.89 g/L. They were 1.81 times higher than that in shake-flask cultivation. The optimization experiment provides the basis for the industrial production of Schizochytrium sp.
[Mh] Termos MeSH primário: Proteínas de Bactérias
Endopeptidases
Extração Líquido-Líquido/métodos
Óleos/isolamento & purificação
Estramenópilas/química
[Mh] Termos MeSH secundário: Ácidos Graxos/análise
Cromatografia Gasosa-Espectrometria de Massas
Concentração de Íons de Hidrogênio
Óleos/química
Estramenópilas/citologia
Temperatura Ambiente
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Fatty Acids); 0 (Oils); EC 3.4.- (Endopeptidases); EC 3.4.99.- (alkaline protease)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180126
[St] Status:MEDLINE
[do] DOI:10.5650/jos.ess17166


  2 / 24575 MEDLINE  
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[PMID]:29335437
[Au] Autor:Zhang S; Zhang M; Jing Y; Yin X; Ma P; Zhang Z; Wang X; Di W; Zhuang G
[Ad] Endereço:State Key Laboratory of Oncogenes and Related Genes, Department of Obstetrics and Gynecology, Ren Ji Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai, 200127, China.
[Ti] Título:Deubiquitinase USP13 dictates MCL1 stability and sensitivity to BH3 mimetic inhibitors.
[So] Source:Nat Commun;9(1):215, 2018 01 15.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:MCL1 is a pivot member of the anti-apoptotic BCL-2 family proteins. While a distinctive feature of MCL1 resides in its efficient ubiquitination and destruction, the deubiquitinase USP9X has been implicated in the preservation of MCL1 expression by removing the polyubiquitin chains. Here we perform an unbiased siRNA screen and identify that the second deubiquitinase, USP13, regulates MCL1 stability in lung and ovarian cancer cells. Mechanistically, USP13 interacts with and stabilizes MCL1 via deubiquitination. As a result, USP13 depletion using CRISPR/Cas9 nuclease system inhibits tumor growth in xenografted nude mice. We further report that genetic or pharmacological inhibition of USP13 considerably reduces MCL1 protein abundance and significantly increases tumor cell sensitivity to BH3 mimetic inhibitors targeting BCL-2 and BCL-XL. Collectively, we nominate USP13 as a novel deubiquitinase which regulates MCL1 turnover in diverse solid tumors and propose that USP13 may be a potential therapeutic target for the treatment of various malignancies.
[Mh] Termos MeSH primário: Endopeptidases/metabolismo
Proteína de Sequência 1 de Leucemia de Células Mieloides/metabolismo
Neoplasias/metabolismo
Ensaios Antitumorais Modelo de Xenoenxerto
[Mh] Termos MeSH secundário: Compostos de Anilina/farmacologia
Animais
Benzilaminas/farmacologia
Sistemas CRISPR-Cas
Linhagem Celular Tumoral
Endopeptidases/genética
Células HEK293
Seres Humanos
Camundongos Endogâmicos BALB C
Camundongos Nus
Proteína de Sequência 1 de Leucemia de Células Mieloides/antagonistas & inibidores
Proteína de Sequência 1 de Leucemia de Células Mieloides/genética
Neoplasias/tratamento farmacológico
Neoplasias/genética
Ligação Proteica
Proteínas Proto-Oncogênicas c-bcl-2/antagonistas & inibidores
Proteínas Proto-Oncogênicas c-bcl-2/metabolismo
Quinazolinas/farmacologia
Interferência de RNA
Sulfonamidas/farmacologia
Ubiquitinação/efeitos dos fármacos
Proteína bcl-X/antagonistas & inibidores
Proteína bcl-X/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Aniline Compounds); 0 (Benzylamines); 0 (MCL1 protein, human); 0 (Myeloid Cell Leukemia Sequence 1 Protein); 0 (Proto-Oncogene Proteins c-bcl-2); 0 (Quinazolines); 0 (Sulfonamides); 0 (bcl-X Protein); 0 (spautin-1); EC 3.4.- (Endopeptidases); EC 3.4.- (USP13 protein, human); XKJ5VVK2WD (navitoclax)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180117
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02693-9


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[PMID]:28470608
[Au] Autor:Raran-Kurussi S; Cherry S; Zhang D; Waugh DS
[Ad] Endereço:Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, B, Frederick, MD, 21702-1201, USA.
[Ti] Título:Removal of Affinity Tags with TEV Protease.
[So] Source:Methods Mol Biol;1586:221-230, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Although affinity tags are highly effective tools for the expression and purification of recombinant proteins, they generally need to be removed prior to structural and functional studies. This chapter describes a simple method for overproducing a soluble form of a stable variant of tobacco etch virus (TEV) protease in Escherichia coli and a protocol for purifying it to homogeneity so that it can be used as a reagent for removing affinity tags from recombinant proteins by site-specific endoproteolysis. Further, we cleave a model substrate protein (MBP-NusG) in vitro using the purified TEV protease to illustrate a protease cleavage protocol that can be employed for simple pilot experiments and large-scale protein preparations.
[Mh] Termos MeSH primário: Cromatografia de Afinidade/métodos
Endopeptidases/genética
Endopeptidases/isolamento & purificação
Escherichia coli/genética
Potyvirus/enzimologia
[Mh] Termos MeSH secundário: Clonagem Molecular/métodos
Endopeptidases/metabolismo
Escherichia coli/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Proteínas Ligantes de Maltose/genética
Proteínas Ligantes de Maltose/metabolismo
Fatores de Alongamento de Peptídeos/genética
Fatores de Alongamento de Peptídeos/metabolismo
Proteólise
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/isolamento & purificação
Proteínas Recombinantes de Fusão/metabolismo
Solubilidade
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Maltose-Binding Proteins); 0 (NusG protein, E coli); 0 (Peptide Elongation Factors); 0 (Recombinant Fusion Proteins); 0 (Transcription Factors); EC 3.4.- (Endopeptidases); EC 3.4.- (TEV protease)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6887-9_14


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[PMID]:29274341
[Au] Autor:DeVine T; Sears RC; Dai MS
[Ad] Endereço:Department of Molecular and Medical Genetics, School of Medicine, The OHSU Knight Cancer Institute, Oregon Health & Science University, Portland, OR, 97239, United States.
[Ti] Título:The ubiquitin-specific protease USP36 is a conserved histone H2B deubiquitinase.
[So] Source:Biochem Biophys Res Commun;495(3):2363-2368, 2018 01 15.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Histone H2B monoubiquitination plays a critical role in the regulation of gene transcription. Deregulation of H2B monoubiquitination contributes to human pathologies, such as cancer. Here we report that human USP36 is a novel H2Bub1 deubiquitinase. We show that USP36 interacts with H2B and deubiquitinates H2Bub1 in cells and in vitro. Overexpression of USP36 markedly reduced the levels of H2Bub1 in cells. Using the p21 gene as a model, we demonstrate that depletion of USP36 increases H2Bub1 at the p21 locus, primarily within its gene body. Consistently, knockdown of USP36 induced the expression of p21 and inhibits cell proliferation. Together, our results reveal USP36 as a novel H2B deubiquitinase and shed light on its additional functions in regulating gene expression.
[Mh] Termos MeSH primário: Enzimas Desubiquitinantes/metabolismo
Endopeptidases/metabolismo
Ubiquitina Tiolesterase/metabolismo
Ubiquitina/metabolismo
Proteínas Ubiquitinadas/metabolismo
Ubiquitinação/fisiologia
[Mh] Termos MeSH secundário: Sequência Conservada
Enzimas Desubiquitinantes/genética
Endopeptidases/genética
Ativação Enzimática
Células HEK293
Células HeLa
Seres Humanos
Ligação Proteica
Especificidade por Substrato
Ubiquitina Tiolesterase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Ubiquitin); 0 (Ubiquitinated Proteins); EC 3.1.2.15 (USP36 protein, human); EC 3.4.- (Endopeptidases); EC 3.4.19.12 (Deubiquitinating Enzymes); EC 3.4.19.12 (Ubiquitin Thiolesterase); EC 3.4.99.- (histone proteases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171224
[St] Status:MEDLINE


  5 / 24575 MEDLINE  
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[PMID]:28450105
[Au] Autor:Rosen O; Feldberg L; Dor E; Gura S; Zichel R
[Ad] Endereço:Department of Biotechnology, Israel Institute for Biological Research, Israel.
[Ti] Título:Optimization of SNAP-25-derived peptide substrate for improved detection of botulinum A in the Endopep-MS assay.
[So] Source:Anal Biochem;528:34-37, 2017 07 01.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Botulinum neurotoxins (BoNTs) are the most toxic proteins in nature. Endopeptidase-mass-spectrometry (Endopep-MS) is used as a specific and rapid in-vitro assay to detect BoNTs. In this assay, immunocaptured toxin cleaves a serotype-specific-peptide-substrate, and the cleavage products are then detected by MS. Here we describe the design of a new peptide substrate for improved detection of BoNT type A (BoNT/A). Our strategy was based on reported BoNT/A-SNAP-25 interactions integrated with analysis method efficiency considerations. Integration of the newly designed substrate led to a 10-fold increase in the assay sensitivity both in buffer and in clinically relevant samples.
[Mh] Termos MeSH primário: Toxinas Botulínicas Tipo A/análise
Espectrometria de Massas/métodos
Peptídeos/análise
Proteína 25 Associada a Sinaptossoma/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Toxinas Botulínicas Tipo A/imunologia
Endopeptidases/metabolismo
Seres Humanos
Peptídeos/química
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); 0 (Synaptosomal-Associated Protein 25); EC 3.4.- (Endopeptidases); EC 3.4.24.69 (Botulinum Toxins, Type A)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE


  6 / 24575 MEDLINE  
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[PMID]:29244473
[Au] Autor:Rotkina AS; Pronina IV; Lazarev VN; Akhaev DN; Baskova IP
[Ti] Título:Destabilase-lysozyme-2 - original recombinant thrombolytic preparation of medicinal leech inhibits horse platelets aggregation.
[So] Source:Patol Fiziol Eksp Ter;60(3):47-51, 2016 Jul-Sep.
[Is] ISSN:0031-2991
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:The purpose. Identifying the capacity of the medicinal leech novel original recombinant thrombolytic preparation Destabilase-Lysozyme-2 to inhibit the blood platelet aggregation. Methods: Gene of destabilase-lysozyme. ds2 (mlDL-Ds2 ), was cloned in E.coli cells. Recombinant protein was isolated in denaturing conditions using metal-chelate chromatography followed by denaturation of the polypeptide by rapid dilution in exact accordance with the procedure described by Kurdyumov A.S. et al. ( 2016, Russian Journal of Bioorganic Chemistry, v.42, s. 42-52). Blood was collected from the jugular vein of 18 horses. The functional status of platelets in the presence of different destabilase-lysozyme concentrations were evaluated for their aggregation in Platelet Rich Plasma ( PRP) and in Washed Platelet suspension (WP) using aggregometers Chrono-Log-700 and Сhrono-Log-560, USA560, США. As used aggregation inducers of ADP, collagen type III and human thrombin. Results: First demonstrated the ability of newly synthesized (Kurdyumov A.S. et al. 2016, Russian Journal of Bioorganic Chemistry, v42, s. 42-52) thrombolytic recombinant enzyme destabilase-lyzosyme to inhibit more than 40% of ADP-stimulated PRP aggregation and ADP- stimulated aggregation of horse blood washed platelets. Conclusion: The ability of destabilase-lyzosyme -2 to inhibit platelets aggregation extends biological properties of recombinant thrombolytic enzyme, pre-clinical trials which resulted in the end of 2015.
[Mh] Termos MeSH primário: Plaquetas/metabolismo
Endopeptidases
Fibrinolíticos
Hirudo medicinalis/enzimologia
Muramidase
Agregação Plaquetária/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Endopeptidases/química
Endopeptidases/isolamento & purificação
Endopeptidases/farmacologia
Fibrinolíticos/química
Fibrinolíticos/isolamento & purificação
Fibrinolíticos/farmacologia
Cavalos
Muramidase/química
Muramidase/isolamento & purificação
Muramidase/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fibrinolytic Agents); EC 3.2.1.17 (Muramidase); EC 3.4.- (Endopeptidases); EC 3.4.99.- (fibrin destabilase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE


  7 / 24575 MEDLINE  
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[PMID]:28464560
[Au] Autor:Wilkinson DJ; Habgood A; Lamb HK; Thompson P; Hawkins AR; Désilets A; Leduc R; Steinmetzer T; Hammami M; Lee MS; Craik CS; Watson S; Lin H; Milner JM; Rowan AD
[Ad] Endereço:Newcastle University, Newcastle upon Tyne, UK.
[Ti] Título:Matriptase Induction of Metalloproteinase-Dependent Aggrecanolysis In Vitro and In Vivo: Promotion of Osteoarthritic Cartilage Damage by Multiple Mechanisms.
[So] Source:Arthritis Rheumatol;69(8):1601-1611, 2017 08.
[Is] ISSN:2326-5205
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To assess the ability of matriptase, a type II transmembrane serine proteinase, to promote aggrecan loss from the cartilage of patients with osteoarthritis (OA) and to determine whether its inhibition can prevent aggrecan loss and cartilage damage in experimental OA. METHODS: Aggrecan release from human OA cartilage explants and human stem cell-derived cartilage discs was evaluated, and cartilage-conditioned media were used for Western blotting. Gene expression was analyzed by real-time polymerase chain reaction. Murine OA was induced by surgical destabilization of the medial meniscus, and matriptase inhibitors were administered via osmotic minipump or intraarticular injection. Cartilage damage was scored histologically and aggrecan cleavage was visualized immunohistochemically using specific neoepitope antibodies. RESULTS: The addition of soluble recombinant matriptase promoted a time-dependent release of aggrecan (and collagen) from OA cartilage, which was sensitive to metalloproteinase inhibition and protease-activated receptor 2 antagonism. Although engineered human (normal) cartilage discs failed to release aggrecan following matriptase addition, both matrix metalloproteinase- and aggrecanase-mediated cleavages of aggrecan were detected in human OA cartilage. Additionally, while matriptase did not directly degrade aggrecan, it promoted the accumulation of low-density lipoprotein receptor-related protein 1 (LRP-1) in conditioned media of the OA cartilage explants. Matriptase inhibition via neutralizing antibody or small molecule inhibitor significantly reduced cartilage damage scores in murine OA, which was associated with reduced generation of metalloproteinase-mediated aggrecan cleavage. CONCLUSION: Matriptase potently induces the release of metalloproteinase-generated aggrecan fragments as well as soluble LRP-1 from OA cartilage. Therapeutic targeting of matriptase proteolytic activity reduces metalloproteinase activity, further suggesting that this serine proteinase may have potential as a disease-modifying therapy in OA.
[Mh] Termos MeSH primário: Agrecanas/efeitos dos fármacos
Cartilagem Articular/efeitos dos fármacos
Osteoartrite do Joelho/metabolismo
Serina Endopeptidases/farmacologia
[Mh] Termos MeSH secundário: Proteína ADAMTS4/efeitos dos fármacos
Proteína ADAMTS4/metabolismo
Proteína ADAMTS5/efeitos dos fármacos
Proteína ADAMTS5/metabolismo
Idoso
Idoso de 80 Anos ou mais
Agrecanas/metabolismo
Animais
Anticorpos Neutralizantes/farmacologia
Western Blotting
Cartilagem Articular/metabolismo
Cartilagem Articular/patologia
Endopeptidases/efeitos dos fármacos
Endopeptidases/metabolismo
Feminino
Perfilação da Expressão Gênica
Seres Humanos
Imuno-Histoquímica
Técnicas In Vitro
Proteína-1 Relacionada a Receptor de Lipoproteína de Baixa Densidade/efeitos dos fármacos
Proteína-1 Relacionada a Receptor de Lipoproteína de Baixa Densidade/metabolismo
Masculino
Metaloproteinases da Matriz/efeitos dos fármacos
Metaloproteinases da Matriz/metabolismo
Proteínas de Membrana/antagonistas & inibidores
Proteínas de Membrana/metabolismo
Meniscos Tibiais/cirurgia
Camundongos
Meia-Idade
Osteoartrite do Joelho/patologia
Reação em Cadeia da Polimerase em Tempo Real
Proteínas Recombinantes/farmacologia
Serina Endopeptidases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Aggrecans); 0 (Antibodies, Neutralizing); 0 (Low Density Lipoprotein Receptor-Related Protein-1); 0 (Membrane Proteins); 0 (Recombinant Proteins); EC 3.4.- (Endopeptidases); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.109 (ST14 protein, human); EC 3.4.21.109 (St14 protein, mouse); EC 3.4.24.- (ADAMTS5 Protein); EC 3.4.24.- (Matrix Metalloproteinases); EC 3.4.24.82 (ADAMTS4 Protein); EC 3.4.99.- (aggrecanase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180119
[Lr] Data última revisão:
180119
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1002/art.40133


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[PMID]:29200282
[Au] Autor:Morgan GJ; Usher GA; Kelly JW
[Ad] Endereço:Departments of Chemistry and Molecular Medicine, and ‡The Skaggs Institute for Chemical Biology, The Scripps Research Institute , La Jolla, California 92037, United States.
[Ti] Título:Incomplete Refolding of Antibody Light Chains to Non-Native, Protease-Sensitive Conformations Leads to Aggregation: A Mechanism of Amyloidogenesis in Patients?
[So] Source:Biochemistry;56(50):6597-6614, 2017 Dec 19.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Genetic, biochemical, and pharmacologic evidence supports the hypothesis that conformationally altered or misfolded protein states enable aggregation and cytotoxicity in the systemic amyloid diseases. Reversible structural fluctuations of natively folded proteins are involved in the aggregation of many degenerative disease associated proteins. Herein, we use antibody light chains (LCs) that form amyloid fibrils in AL amyloidosis to consider an alternative hypothesis of amyloidogenesis: that transient unfolding and incomplete extracellular refolding of secreted proteins can lead to metastable, alternatively folded states that are more susceptible to aggregation or to endoproteolysis that can release aggregation-prone fragments. Refolding of full-length λ6a LC dimers comprising an interchain disulfide bond from heat- or chaotrope-denatured ensembles in buffers yields the native dimeric state as well as alternatively folded dimers and aggregates. LC variants lacking an interchain disulfide bond appear to refold fully reversibly to the native state. The conformation of a backbone peptidyl-proline amide in the LC constant domain, which is cis in the native state, may determine whether the LC refolds back to the native state. A proline to alanine (P147A) LC variant, which cannot form the native cis-amide conformation, forms amyloid fibrils from the alternatively folded ensemble, whereas all the full-length λ6a LCs we have studied to date do not form amyloid under analogous conditions. P147A LC variants are susceptible to endoproteolysis by thrombin, enabling amyloidogenesis of the fragments released. Thus, non-native LC structural ensembles containing a tyrosine 146-proline 147 trans-amide bond can initiate and propagate amyloid formation, either directly or after aberrant endoproteolysis.
[Mh] Termos MeSH primário: Amiloidose/metabolismo
Cadeias Leves de Imunoglobulina/química
Cadeias Leves de Imunoglobulina/metabolismo
[Mh] Termos MeSH secundário: Alanina/química
Amiloide/química
Dicroísmo Circular
Endopeptidases/metabolismo
Seres Humanos
Cadeias Leves de Imunoglobulina/genética
Cinética
Modelos Moleculares
Prolina/química
Agregados Proteicos/fisiologia
Conformação Proteica
Dobramento de Proteína
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid); 0 (Immunoglobulin Light Chains); 0 (Protein Aggregates); 9DLQ4CIU6V (Proline); EC 3.4.- (Endopeptidases); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00579


  9 / 24575 MEDLINE  
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[PMID]:29190780
[Au] Autor:Saggu SK; Mishra PC
[Ad] Endereço:Department of Biotechnology, Guru Nanak Dev University, Amritsar, Punjab, India.
[Ti] Título:Characterization of thermostable alkaline proteases from Bacillus infantis SKS1 isolated from garden soil.
[So] Source:PLoS One;12(11):e0188724, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proteases are one of the largest groups of hydrolytic enzymes constituting about 60% of total worldwide sales of industrial enzymes due to their wide applications in detergent, leather, textile, food and pharmaceutical industry. Microbial proteases have been preferred over animal and plant proteases because of their fundamental features and ease in production. Bacillus infantis SKS1, an alkaline protease producing bacteria has been isolated from garden soil of north India and identified using morphological, biochemical and molecular methods. 16S rDNA sequence amplified using universal primers has 99% sequence identity with corresponding gene sequence of Bacillus infantis strain FM 34 and Bacillus sp. Beige. The bacterial culture and its 16S rDNA gene sequence have been deposited to Microbial Culture Collection (Pune, India) with accession number MCC 3035 and GenBank with accession number KR092197 respectively. The partially purified extract of Bacillus infantis SKS1 was thermostable and active in presence of Mg2+, acetyl acetone and laundry detergents implicating its application in industry. Production of these enzymes using this strain was maximized by optimization of various parameters including temperature, pH, media components and other growth conditions. Our results show that fructose and dextrose serve as the best carbon sources for production of these enzymes, highlighting the use of this strain for enzyme production utilizing relatively inexpensive substrates like beet molasses and corn steep liquor. Additionally, this strain showed maximum production of enzymes at 40°C similar to bacterial species used for commercial production of alkaline proteases. Characterization of alkaline proteases from this strain of Bacillus infantis and optimization of parameters for its production would help in understanding its industrial application and large-scale production.
[Mh] Termos MeSH primário: Bacillus/enzimologia
Proteínas de Bactérias/metabolismo
Endopeptidases/metabolismo
Microbiologia do Solo
[Mh] Termos MeSH secundário: Detergentes/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Detergents); EC 3.4.- (Endopeptidases); EC 3.4.99.- (alkaline protease)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188724


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[PMID]:27776223
[Au] Autor:Zhang Q; Wang Z; Hou F; Harding R; Huang X; Dong A; Walker JR; Tong Y
[Ad] Endereço:Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7, Canada.
[Ti] Título:The substrate binding domains of human SIAH E3 ubiquitin ligases are now crystal clear.
[So] Source:Biochim Biophys Acta;1861(1 Pt A):3095-3105, 2017 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Seven in absentia homologs (SIAHs) comprise a family of highly conserved E3 ubiquitin ligases that play an important role in regulating signalling pathways in tumorigenesis, including the DNA damage repair and hypoxia response pathways. SIAH1 and SIAH2 have been found to function as a tumour repressor and a proto-oncogene, respectively, despite the high sequence identity of their substrate binding domains (SBDs). Ubiquitin-specific protease USP19 is a deubiquitinase that forms a complex with SIAHs and counteracts the ligase function. Much effort has been made to find selective inhibitors of the SIAHs E3 ligases. Menadione was reported to inhibit SIAH2 specifically. METHODS: We used X-ray crystallography, peptide array, bioinformatic analysis, and biophysical techniques to characterize the structure and interaction of SIAHs with deubiquitinases and literature reported compounds. RESULTS: We solved the crystal structures of SIAH1 in complex with a USP19 peptide and of the apo form SIAH2. Phylogenetic analysis revealed the SIAH/USP19 complex is conserved in evolution. We demonstrated that menadione destabilizes both SIAH1 and SIAH2 non-specifically through covalent modification. CONCLUSIONS: The SBDs of SIAH E3 ligases are structurally similar with a subtle stability difference. USP19 is the only deubiquitinase that directly binds to SIAHs through the substrate binding pocket. Menadione is not a specific inhibitor for SIAH2. GENERAL SIGNIFICANCE: The crystallographic models provide structural insights into the substrate binding of the SIAH family E3 ubiquitin ligases that are critically involved in regulating cancer-related pathways. Our results suggest caution should be taken when using menadione as a specific SIAH2 inhibitor.
[Mh] Termos MeSH primário: Proteínas Nucleares/química
Ubiquitina-Proteína Ligases/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Carcinogênese/metabolismo
Carcinogênese/patologia
Cristalografia por Raios X
Endopeptidases/metabolismo
Evolução Molecular
Seres Humanos
Modelos Moleculares
Proteínas Nucleares/antagonistas & inibidores
Filogenia
Ligação Proteica
Domínios Proteicos
Estabilidade Proteica/efeitos dos fármacos
Estrutura Secundária de Proteína
Especificidade por Substrato/efeitos dos fármacos
Ubiquitina-Proteína Ligases/antagonistas & inibidores
Vitamina K 3/farmacologia
[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 (Nuclear Proteins); 723JX6CXY5 (Vitamin K 3); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.3.2.27 (seven in absentia proteins); EC 3.4.- (Endopeptidases); EC 3.4.- (USP19 protein, human)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171224
[Lr] Data última revisão:
171224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161107
[St] Status:MEDLINE



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