Base de dados : MEDLINE
Pesquisa : D12.776.090 [Categoria DeCS]
Referências encontradas : 5235 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 524 ir para página                         

  1 / 5235 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28993252
[Au] Autor:Berry L; Poudel S; Tokmina-Lukaszewska M; Colman DR; Nguyen DMN; Schut GJ; Adams MWW; Peters JW; Boyd ES; Bothner B
[Ad] Endereço:Montana State University, Bozeman, MT 59717, United States. Electronic address: Lukeberry15@gmail.com.
[Ti] Título:H/D exchange mass spectrometry and statistical coupling analysis reveal a role for allostery in a ferredoxin-dependent bifurcating transhydrogenase catalytic cycle.
[So] Source:Biochim Biophys Acta;1862(1):9-17, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Recent investigations into ferredoxin-dependent transhydrogenases, a class of enzymes responsible for electron transport, have highlighted the biological importance of flavin-based electron bifurcation (FBEB). FBEB generates biomolecules with very low reduction potential by coupling the oxidation of an electron donor with intermediate potential to the reduction of high and low potential molecules. Bifurcating systems can generate biomolecules with very low reduction potentials, such as reduced ferredoxin (Fd), from species such as NADPH. Metabolic systems that use bifurcation are more efficient and confer a competitive advantage for the organisms that harbor them. Structural models are now available for two NADH-dependent ferredoxin-NADP oxidoreductase (Nfn) complexes. These models, together with spectroscopic studies, have provided considerable insight into the catalytic process of FBEB. However, much about the mechanism and regulation of these multi-subunit proteins remains unclear. Using hydrogen/deuterium exchange mass spectrometry (HDX-MS) and statistical coupling analysis (SCA), we identified specific pathways of communication within the model FBEB system, Nfn from Pyrococus furiosus, under conditions at each step of the catalytic cycle. HDX-MS revealed evidence for allosteric coupling across protein subunits upon nucleotide and ferredoxin binding. SCA uncovered a network of co-evolving residues that can provide connectivity across the complex. Together, the HDX-MS and SCA data show that protein allostery occurs across the ensemble of iron­sulfur cofactors and ligand binding sites using specific pathways that connect domains allowing them to function as dynamically coordinated units.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Medição da Troca de Deutério/métodos
Ferredoxinas/química
NADP Trans-Hidrogenases/química
Pyrococcus furiosus/enzimologia
[Mh] Termos MeSH secundário: Regulação Alostérica
Proteínas Arqueais/metabolismo
Ferredoxinas/metabolismo
NADP Trans-Hidrogenases/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 (Archaeal Proteins); 0 (Ferredoxins); EC 1.6.1.- (NADP Transhydrogenases)
[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:171011
[St] Status:MEDLINE


  2 / 5235 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29199993
[Au] Autor:Pampa KJ; Madan Kumar S; Hema MK; Kumara K; Naveen S; Kunishima N; Lokanath NK
[Ad] Endereço:Department of Studies in Biotechnology, University of Mysore, Manasagangotri, Mysuru, Karnataka 570 006, India.
[Ti] Título:Crystal structure of SAM-dependent methyltransferase from Pyrococcus horikoshii.
[So] Source:Acta Crystallogr F Struct Biol Commun;73(Pt 12):706-712, 2017 Dec 01.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Methyltransferases (MTs) are enzymes involved in methylation that are needed to perform cellular processes such as biosynthesis, metabolism, gene expression, protein trafficking and signal transduction. The cofactor S-adenosyl-L-methionine (SAM) is used for catalysis by SAM-dependent methyltransferases (SAM-MTs). The crystal structure of Pyrococcus horikoshii SAM-MT was determined to a resolution of 2.1 Šusing X-ray diffraction. The monomeric structure consists of a Rossmann-like fold (domain I) and a substrate-binding domain (domain II). The cofactor (SAM) molecule binds at the interface between adjacent subunits, presumably near to the active site(s) of the enzyme. The observed dimeric state might be important for the catalytic function of the enzyme.
[Mh] Termos MeSH primário: Metiltransferases/química
Metiltransferases/metabolismo
Pyrococcus horikoshii/enzimologia
S-Adenosilmetionina/metabolismo
[Mh] Termos MeSH secundário: Proteínas Arqueais/química
Proteínas Arqueais/metabolismo
Sítios de Ligação
Cristalografia por Raios X
Modelos Moleculares
Conformação Proteica
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 7LP2MPO46S (S-Adenosylmethionine); EC 2.1.1.- (Methyltransferases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X17016648


  3 / 5235 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28470611
[Au] Autor:Love JD
[Ad] Endereço:Department of Biochemistry, Albert Einstein College of Medicine at Yeshiva University, Bronx, NY, USA. drjamesdlove@gmail.com.
[Ti] Título:Expression of Prokaryotic Integral Membrane Proteins in E. coli.
[So] Source:Methods Mol Biol;1586:265-278, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Production of prokaryotic membrane proteins for structural and functional studies in E. coli can be parallelized and miniaturized. All stages from cloning, expression, purification to detergent selection can be investigated using high-throughput techniques to rapidly and economically find tractable targets.
[Mh] Termos MeSH primário: Proteínas Arqueais/genética
Proteínas de Bactérias/genética
Clonagem Molecular/métodos
Escherichia coli/genética
Proteínas de Membrana/genética
[Mh] Termos MeSH secundário: Proteínas Arqueais/química
Proteínas Arqueais/isolamento & purificação
Bactérias/genética
Proteínas de Bactérias/química
Proteínas de Bactérias/isolamento & purificação
Detergentes/química
Expressão Gênica
Vetores Genéticos/genética
Proteínas de Membrana/química
Proteínas de Membrana/isolamento & purificação
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Bacterial Proteins); 0 (Detergents); 0 (Membrane Proteins); 0 (Recombinant Proteins)
[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_17


  4 / 5235 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29284023
[Au] Autor:Kosugi N; Araki T; Fujita J; Tanaka S; Fujiwara T
[Ad] Endereço:Department of Science, Graduate School of Integrated Science and Technology, Shizuoka University, Shizuoka, Japan.
[Ti] Título:Growth phenotype analysis of heme synthetic enzymes in a halophilic archaeon, Haloferax volcanii.
[So] Source:PLoS One;12(12):e0189913, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Halophilic euryarchaea lack many of the genes necessary for the protoporphyrin-dependent heme biosynthesis pathway previously identified in animals and plants. Bioinformatic analysis suggested the presence of two heme biosynthetic processes, an Fe-coproporphyrinogen III (coproheme) decarboxylase (ChdC) pathway and an alternative heme biosynthesis (Ahb) pathway, in Haloferax volcanii. PitA is specific to the halophilic archaea and has a unique molecular structure in which the ChdC domain is joined to the antibiotics biosynthesis monooxygenase (ABM)-like domain by a histidine-rich linker sequence. The pitA gene deletion variant of H. volcanii showed a phenotype with a significant reduction of aerobic growth. Addition of a protoheme complemented the phenotype, supporting the assumption that PitA participates in the aerobic heme biosynthesis. Deletion of the ahbD gene caused a significant reduction of only anaerobic growth by denitrification or dimethylsulfoxide (DMSO) respiration, and the growth was also complemented by addition of a protoheme. The experimental results suggest that the two heme biosynthesis pathways are utilized selectively under aerobic and anaerobic conditions in H. volcanii. The molecular structure and physiological function of PitA are also discussed on the basis of the limited proteolysis and sequence analysis.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
Haloferax volcanii/crescimento & desenvolvimento
Heme/metabolismo
[Mh] Termos MeSH secundário: Deleção de Genes
Regulação da Expressão Gênica em Archaea
Haloferax volcanii/enzimologia
Haloferax volcanii/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 42VZT0U6YR (Heme)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171229
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189913


  5 / 5235 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27771939
[Au] Autor:Hoffmann L; Schummer A; Reimann J; Haurat MF; Wilson AJ; Beeby M; Warscheid B; Albers SV
[Ad] Endereço:Molecular Biology of Archaea, Institute of Biology II, Faculty of Biology, Microbiology, University of Freiburg, Freiburg, Germany.
[Ti] Título:Expanding the archaellum regulatory network - the eukaryotic protein kinases ArnC and ArnD influence motility of Sulfolobus acidocaldarius.
[So] Source:Microbiologyopen;6(1), 2017 02.
[Is] ISSN:2045-8827
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Expression of the archaellum, the archaeal-type IV pilus-like rotating motility structure is upregulated under nutrient limitation. This is controlled by a network of regulators, called the archaellum regulatory network (arn). Several of the components of this network in Sulfolobus acidocaldarius can be phosphorylated, and the deletion of the phosphatase PP2A results in strongly increased motility during starvation, indicating a role for phosphorylation in the regulation of motility. Analysis of the motility of different protein kinase deletion strains revealed that deletion of saci_0965, saci_1181, and saci_1193 resulted in reduced motility, whereas the deletion of saci_1694 resulted in hypermotility. Here ArnC (Saci_1193) and ArnD (Saci_1694) are characterized. Purified ArnC and ArnD phosphorylate serine and threonine residues in the C-terminus of the repressor ArnB. arnC is upregulated in starvation medium, whereas arnD is constitutively expressed. However, while differences in the expression and levels of flaB were observed in the ΔarnD strain during growth under rich conditions, under nutrient limiting conditions the ΔarnC and ΔarnD strains showed no large differences in the expression levels of the archaellum or of the studied regulators. This suggests that next to the regulation via the archaellum regulatory network additional regulatory mechanisms of expression and/or activity of the archaellum exist.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
Flagelos/metabolismo
Regulação da Expressão Gênica em Archaea
Proteínas Quinases/metabolismo
Sulfolobus acidocaldarius/metabolismo
[Mh] Termos MeSH secundário: Proteínas Arqueais/genética
Flagelos/genética
Deleção de Genes
Fosforilação
Domínios Proteicos
Proteínas Quinases/genética
Transdução de Sinais/fisiologia
Inanição
Sulfolobus acidocaldarius/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); EC 2.7.- (Protein Kinases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE
[do] DOI:10.1002/mbo3.414


  6 / 5235 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27773688
[Au] Autor:Nakae S; Hijikata A; Tsuji T; Yonezawa K; Kouyama KI; Mayanagi K; Ishino S; Ishino Y; Shirai T
[Ad] Endereço:Department of Bioscience, Nagahama Institute of Bio-Science and Technology, Tamura 1266, Nagahama, Shiga 526-0829, Japan.
[Ti] Título:Structure of the EndoMS-DNA Complex as Mismatch Restriction Endonuclease.
[So] Source:Structure;24(11):1960-1971, 2016 11 01.
[Is] ISSN:1878-4186
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Archaeal NucS nuclease was thought to degrade the single-stranded region of branched DNA, which contains flapped and splayed DNA. However, recent findings indicated that EndoMS, the orthologous enzyme of NucS, specifically cleaves double-stranded DNA (dsDNA) containing mismatched bases. In this study, we determined the structure of the EndoMS-DNA complex. The complex structure of the EndoMS dimer with dsDNA unexpectedly revealed that the mismatched bases were flipped out into binding sites, and the overall architecture most resembled that of restriction enzymes. The structure of the apo form was similar to the reported structure of Pyrococcus abyssi NucS, indicating that movement of the C-terminal domain from the resting state was required for activity. In addition, a model of the EndoMS-PCNA-DNA complex was preliminarily verified with electron microscopy. The structures strongly support the idea that EndoMS acts in a mismatch repair pathway.
[Mh] Termos MeSH primário: DNA de Cadeia Simples/metabolismo
Endodesoxirribonucleases/química
Endodesoxirribonucleases/metabolismo
Pyrococcus abyssi/enzimologia
[Mh] Termos MeSH secundário: Proteínas Arqueais/química
Proteínas Arqueais/metabolismo
Sítios de Ligação
Reparo de Erro de Pareamento de DNA
DNA Arqueal/química
DNA Arqueal/metabolismo
DNA de Cadeia Simples/química
Microscopia Eletrônica
Modelos Moleculares
Ligação Proteica
Conformação Proteica
Pyrococcus abyssi/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (DNA, Archaeal); 0 (DNA, Single-Stranded); EC 3.1.- (Endodeoxyribonucleases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171230
[Lr] Data última revisão:
171230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161103
[St] Status:MEDLINE


  7 / 5235 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28471363
[Au] Autor:Sivaji N; Abhinav KV; Vijayan M
[Ad] Endereço:Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
[Ti] Título:Crystallization and biochemical characterization of an archaeal lectin from Methanococcus voltae A3.
[So] Source:Acta Crystallogr F Struct Biol Commun;73(Pt 5):300-304, 2017 May 01.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A lectin from Methanococcus voltae A3 has been cloned, expressed, purified and characterized. The lectin appears to be specific for complex sugars. The protein crystallized in a tetragonal space group, with around 16 subunits in the asymmetric unit. Sequence comparisons indicate the lectin to have a ß-prism I fold, with poor homology to lectins of known three-dimensional structure.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Lectinas/química
Mathanococcus/química
Subunidades Proteicas/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas Arqueais/genética
Proteínas Arqueais/metabolismo
Clonagem Molecular
Cristalização
Cristalografia por Raios X
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Vetores Genéticos/química
Vetores Genéticos/metabolismo
Lectinas/genética
Lectinas/metabolismo
Mathanococcus/metabolismo
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Lectins); 0 (Protein Subunits); 0 (Recombinant Fusion Proteins)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171204
[Lr] Data última revisão:
171204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X17006173


  8 / 5235 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28965803
[Au] Autor:Sui Y; Fu X; Wang Y; Hu W; Zhang T; Liu W; Jiang L; Xing S; Fu X; Xu X
[Ad] Endereço:Edmond H. Fischer Signal Transduction Laboratory, School of Life Sciences, Jilin University, Changchun 130012, PR China.
[Ti] Título:Expression, purification and characterization of a catalytic domain of human protein tyrosine phosphatase non-receptor 12 (PTPN12) in Escherichia coli with FKBP-type PPIase as a chaperon.
[So] Source:Protein Expr Purif;142:45-52, 2018 Feb.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein tyrosine phosphatase non-receptor type 12 (PTPN12), also known as PTP-PEST, was broadly expressed in hemopoietic cells. Recent research has shown that this enzyme is involved in tumorigenesis, as well as in tumor progression and transfer, as it can suppress multiple oncogenic tyrosine kinases. However, the difficulty of soluble expression of PTP-PEST in prokaryotic cells has resulted in great limitations in investigating its structure and functions. In this study, we successfully carried out soluble expression of the catalytic domain of PTP-PEST (ΔPTP-PEST) in Escherichia coli and performed an enzymatic characterization and kinetics. To confirm expression efficiency, we also induced the expression of the chaperon, FKBP_C. FKBP_C expression indicated efficacious prokaryotic expression of ΔPTP-PEST. In conclusion, our work yielded a practical expression system and two-step chromatography purification method that may serve as a valuable tool for the structural and functional analysis of proteins that are difficult to express in the soluble form in prokaryotic cells.
[Mh] Termos MeSH primário: Proteínas Arqueais/genética
Chaperonas Moleculares/genética
Peptidilprolil Isomerase/genética
Proteína Tirosina Fosfatase não Receptora Tipo 12/genética
Proteínas de Ligação a Tacrolimo/genética
Thermococcus/química
[Mh] Termos MeSH secundário: Proteínas Arqueais/metabolismo
Domínio Catalítico
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Seres Humanos
Cinética
Chaperonas Moleculares/metabolismo
Peptidilprolil Isomerase/metabolismo
Plasmídeos/química
Plasmídeos/metabolismo
Proteína Tirosina Fosfatase não Receptora Tipo 12/isolamento & purificação
Proteína Tirosina Fosfatase não Receptora Tipo 12/metabolismo
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Proteínas de Ligação a Tacrolimo/metabolismo
Thermococcus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Molecular Chaperones); 0 (Recombinant Fusion Proteins); EC 3.1.3.48 (PTPN12 protein, human); EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 12); EC 5.2.1.- (Tacrolimus Binding Proteins); EC 5.2.1.8 (Peptidylprolyl Isomerase)
[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:171003
[St] Status:MEDLINE


  9 / 5235 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28743912
[Au] Autor:Gandini R; Reichenbach T; Tan TC; Divne C
[Ad] Endereço:School of Biotechnology, KTH Royal Institute of Technology, S-10691, Stockholm, Sweden.
[Ti] Título:Structural basis for dolichylphosphate mannose biosynthesis.
[So] Source:Nat Commun;8(1):120, 2017 07 25.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Protein glycosylation is a critical protein modification. In biogenic membranes of eukaryotes and archaea, these reactions require activated mannose in the form of the lipid conjugate dolichylphosphate mannose (Dol-P-Man). The membrane protein dolichylphosphate mannose synthase (DPMS) catalyzes the reaction whereby mannose is transferred from GDP-mannose to the dolichol carrier Dol-P, to yield Dol-P-Man. Failure to produce or utilize Dol-P-Man compromises organism viability, and in humans, several mutations in the human dpm1 gene lead to congenital disorders of glycosylation (CDG). Here, we report three high-resolution crystal structures of archaeal DPMS from Pyrococcus furiosus, in complex with nucleotide, donor, and glycolipid product. The structures offer snapshots along the catalytic cycle, and reveal how lipid binding couples to movements of interface helices, metal binding, and acceptor loop dynamics to control critical events leading to Dol-P-Man synthesis. The structures also rationalize the loss of dolichylphosphate mannose synthase function in dpm1-associated CDG.The generation of glycolipid dolichylphosphate mannose (Dol-P-Man) is a critical step for protein glycosylation and GPI anchor synthesis. Here the authors report the structure of dolichylphosphate mannose synthase in complex with bound nucleotide and donor to provide insight into the mechanism of Dol-P-Man synthesis.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
Manose/biossíntese
Manosiltransferases/metabolismo
Pyrococcus furiosus/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas Arqueais/química
Proteínas Arqueais/genética
Sítios de Ligação/genética
Biocatálise
Cristalografia por Raios X
Manose/química
Manosiltransferases/química
Manosiltransferases/genética
Modelos Moleculares
Domínios Proteicos
Pyrococcus furiosus/enzimologia
Pyrococcus furiosus/genética
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Recombinant Proteins); EC 2.4.1.- (Mannosyltransferases); EC 2.4.1.109 (protein O-mannosyltransferase); PHA4727WTP (Mannose)
[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:170727
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-00187-2


  10 / 5235 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28982174
[Au] Autor:Concha-Marambio L; Maldonado P; Lagos R; Monasterio O; Montecinos-Franjola F
[Ad] Endereço:Laboratorio de Biologia Estructural y Molecular/Departamento de Biologia/Facultad de Ciencias, Universidad de Chile, Santiago, Chile.
[Ti] Título:Thermal adaptation of mesophilic and thermophilic FtsZ assembly by modulation of the critical concentration.
[So] Source:PLoS One;12(10):e0185707, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cytokinesis is the last stage in the cell cycle. In prokaryotes, the protein FtsZ guides cell constriction by assembling into a contractile ring-shaped structure termed the Z-ring. Constriction of the Z-ring is driven by the GTPase activity of FtsZ that overcomes the energetic barrier between two protein conformations having different propensities to assemble into polymers. FtsZ is found in psychrophilic, mesophilic and thermophilic organisms thereby functioning at temperatures ranging from subzero to >100°C. To gain insight into the functional adaptations enabling assembly of FtsZ in distinct environmental conditions, we analyzed the energetics of FtsZ function from mesophilic Escherichia coli in comparison with FtsZ from thermophilic Methanocaldococcus jannaschii. Presumably, the assembly may be similarly modulated by temperature for both FtsZ orthologs. The temperature dependence of the first-order rates of nucleotide hydrolysis and of polymer disassembly, indicated an entropy-driven destabilization of the FtsZ-GTP intermediate. This destabilization was true for both mesophilic and thermophilic FtsZ, reflecting a conserved mechanism of disassembly. From the temperature dependence of the critical concentrations for polymerization, we detected a change of opposite sign in the heat capacity, that was partially explained by the specific changes in the solvent-accessible surface area between the free and polymerized states of FtsZ. At the physiological temperature, the assembly of both FtsZ orthologs was found to be driven by a small positive entropy. In contrast, the assembly occurred with a negative enthalpy for mesophilic FtsZ and with a positive enthalpy for thermophilic FtsZ. Notably, the assembly of both FtsZ orthologs is characterized by a critical concentration of similar value (1-2 µM) at the environmental temperatures of their host organisms. These findings suggest a simple but robust mechanism of adaptation of FtsZ, previously shown for eukaryotic tubulin, by adjustment of the critical concentration for polymerization.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
Methanocaldococcus/metabolismo
[Mh] Termos MeSH secundário: Biopolímeros/metabolismo
Escherichia coli/genética
Guanosina Trifosfato/metabolismo
Hidrólise
Cinética
Methanocaldococcus/genética
Polimerização
Temperatura Ambiente
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Biopolymers); 0 (FtsZ protein, Methanococcus jannaschii); 86-01-1 (Guanosine Triphosphate)
[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:171006
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185707



página 1 de 524 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde