Search results for "030302 biochemistry & molecular biology"

showing 10 items of 238 documents

Binding and/or hydrolysis of purine‐based nucleotides is not required for IM30 ring formation

2021

IM30, the inner membrane-associated protein of 30 kDa, is conserved in cyanobacteria and chloroplasts. Although its exact physiological function is still mysterious, IM30 is clearly essential for thylakoid membrane biogenesis and/or dynamics. Recently, a cryptic IM30 GTPase activity has been reported, albeit thus far no physiological function has been attributed to this. Yet, it is still possible that GTP binding/hydrolysis affects formation of the prototypical large homo-oligomeric IM30 ring and rod structures. Here, we show that the Synechocystis sp. PCC 6803 IM30 protein in fact is an NTPase that hydrolyzes GTP and ATP, but not CTP or UTP, with about identical rates. While IM30 forms lar…

GTP'Genetic VectorsBiophysicsGene ExpressionGTPaseRing (chemistry)ThylakoidsBiochemistrySubstrate Specificity03 medical and health sciencesAdenosine TriphosphateBacterial ProteinsStructural BiologyEscherichia coliGeneticsNucleotideddc:610Cloning MolecularMolecular BiologyEnzyme Assays030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyChemistryHydrolysis030302 biochemistry & molecular biologySynechocystisSynechocystisMembrane ProteinsCell BiologyNucleoside-Triphosphatasebiology.organism_classificationRecombinant ProteinsKineticsMicroscopy ElectronThylakoidMembrane biogenesisBiophysicsGuanosine TriphosphateBiogenesisProtein BindingFEBS Letters
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Evolutionary plasticity of SH3 domain binding by Nef proteins of the HIV-1/SIVcpz lentiviral lineage

2021

ABSTRACTThe accessory protein Nef of human and simian immunodeficiency viruses (HIV and SIV) is an important pathogenicity factor known to interact with cellular protein kinases and other signaling proteins. A canonical SH3 domain binding motif in Nef is required for most of these interactions. For example, HIV-1 Nef activates the tyrosine kinase Hck by tightly binding to its SH3 domain. An archetypal contact between a negatively charged SH3 residue and a highly conserved arginine in Nef (Arg77) plays a key role here. Combining structural analyses with functional assays, we here show that Nef proteins have also developed a distinct structural strategy - termed the “R-clamp” - that favors th…

Geneticschemistry.chemical_classification0303 health sciencesLineage (genetic)Kinaseviruses030302 biochemistry & molecular biologyHuman immunodeficiency virus (HIV)virus diseasesBiologymedicine.disease_causeSH3 domainAmino acid03 medical and health scienceschemistrymedicineSalt bridgeBinding siteTyrosine kinase030304 developmental biology
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Role of the Netrin-like Domain of Procollagen C-Proteinase Enhancer-1 in the Control of Metalloproteinase Activity

2010

The netrin-like (NTR) domain is a feature of several extracellular proteins, most notably the N-terminal domain of tissue inhibitors of metalloproteinases (TIMPs), where it functions as a strong inhibitor of matrix metalloproteinases and some other members of the metzincin superfamily. The presence of a C-terminal NTR domain in procollagen C-proteinase enhancers (PCPEs), proteins that stimulate the activity of astacin-like tolloid proteinases, raises the possibility that this might also have inhibitory activity. Here we show that both long and short forms of the PCPE-1 NTR domain, the latter beginning at the N-terminal cysteine known to be critical for TIMP activity, show no inhibition, at …

Glycobiology and Extracellular MatricesMatrix metalloproteinaseBiochemistryBONE MORPHOGENETIC PROTEIN-1AdamalysinFIBRILLAR PROCOLLAGENSTolloid ProteinaseExtracellular Matrix Proteins0303 health sciencesADAMTSFRIZZLED-RELATED PROTEINS030302 biochemistry & molecular biologyTissue Inhibitor of Metalloproteinases11 Medical And Health SciencesALPHA-CONVERTING-ENZYMEI PROCOLLAGENADAM ProteinsExtracellular MatrixPLASMINOGEN ACTIVATIONBiochemistryCollagen03 Chemical SciencesLife Sciences & BiomedicineProcollagenBiochemistry & Molecular BiologyTERMINAL DOMAINTolloid-Like MetalloproteinasesADAMTSBiologyBone morphogenetic protein 1Cell Line03 medical and health sciencesDisintegrinHumansHUMAN TISSUE INHIBITORMatrix MetalloproteinaseMolecular BiologyGlycoproteins030304 developmental biologyThrombospondinScience & TechnologyHeparinADAMCell Biology06 Biological SciencesMATRIX-METALLOPROTEINASESProtein Structure TertiaryADAM ProteinsProcollagen peptidaseSULFATED GLYCOSAMINOGLYCANSEnzymologybiology.proteinJournal of Biological Chemistry
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The shell-forming proteome of Lottia gigantea reveals both deep conservations and lineage-specific novelties

2013

19 pages; International audience; Proteins that are occluded within the molluscan shell, the so-called shell matrix proteins (SMPs), are an assemblage of biomolecules attractive to study for several reasons. They increase the fracture resistance of the shell by several orders of magnitude, determine the polymorph of CaCO(3) deposited, and regulate crystal nucleation, growth initiation and termination. In addition, they are thought to control the shell microstructures. Understanding how these proteins have evolved is also likely to provide deep insight into events that supported the diversification and expansion of metazoan life during the Cambrian radiation 543 million years ago. Here, we p…

Glycoside Hydrolasesmedicine.medical_treatmentproteomeGastropodaMolecular Sequence DataBiologyBiochemistrymollusc shell matrix proteinsTranscriptomeCyclophilins03 medical and health sciencesPaleontologyLineage specificAnimal ShellsSequence Analysis ProteinTandem Mass Spectrometry[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]evolutionmedicineAnimalsAmino Acid Sequence14. Life underwaterMantle (mollusc)[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular BiologyCarbonic Anhydrases030304 developmental biologyExtracellular Matrix Proteins0303 health sciencesProteaseEpidermal Growth FactorSequence Homology Amino AcidLimpet030302 biochemistry & molecular biologyCell Biologybiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsbiomineralizationPeptide FragmentsProtein Structure TertiaryPeroxidasesEvolutionary biology[ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]ProteomeLottia giganteaElectrophoresis Polyacrylamide GelmantleBiomineralization
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Phospholipid distribution in the cytoplasmic membrane of Gram-negative bacteria is highly asymmetric, dynamic, and cell shape-dependent

2020

The cell shape of Gram-negative bacteria is maintained metabolically by asymmetric lipid distribution in biogenic plasma membrane.

Gram-negative bacteriaPhospholipidBiochemistryMicrobiology03 medical and health scienceschemistry.chemical_compoundGram-Negative BacteriaCardiolipinEscherichia coliInner membraneCell ShapePhospholipidsResearch Articles030304 developmental biologyPhosphatidylethanolamine0303 health sciencesMultidisciplinarybiologyBilayer030302 biochemistry & molecular biologyCell MembraneSciAdv r-articlesPeriplasmic spacebiology.organism_classificationchemistryCytoplasmBiophysicslipids (amino acids peptides and proteins)Research Article
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5-methylcytosine modification of an Epstein–Barr virus noncoding RNA decreases its stability

2020

Many cellular noncoding RNAs contain chemically modified nucleotides that are essential for their function. The Epstein–Barr virus expresses two highly abundant noncoding RNAs called EBV-encoded RNA 1 (EBER1) and EBER2. To examine whether these viral RNAs contain modified nucleotides, we purified native EBERs from EBV-infected cells and performed mass spectrometry analysis. While EBER2 contains no modified nucleotides at stoichiometric amounts, EBER1 was found to carry 5-methylcytosine (m5C) modification. Bisulfite sequencing indicated that a single cytosine of EBER1 is methylated in ∼95% of molecules, and the RNA methyltransferase NSUN2 was identified as the EBER1-specific writer. Intrigui…

Herpesvirus 4 HumanRNA StabilityRNA UntranslatedRNase PRNA StabilityBisulfite sequencingBiologyArticle03 medical and health scienceschemistry.chemical_compoundhemic and lymphatic diseasesHumansNucleotideMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciences030302 biochemistry & molecular biologyvirus diseasesRNAMethyltransferasesNon-coding RNA5-MethylcytosineBiochemistrychemistry5-MethylcytosineRNA ViralCytosineRNA
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Gene Expression and Epigenetic Signatures of Germ Cell-Derived Pluripotent Stem Cells and Embryonic Stem Cells

2012

Germ cell-derived Pluripotent Stem Cells (gPSCs) are pluripotent stem cells that originate from Spermatogonial Stem Cells (SSCs) of the testis. Several reports in the last few years have shown that it is possible to isolate and enrich the SSC population by different approaches and even reprogram these in vivo multipotent cells to gPSCs in vitro. As these cells could be an alternative to circumvent the ethical objections regarding the use of Embryonic Stem Cells (ESCs) for therapeutic approaches, these SSC-derived gPSCs were characterized in several studies comparatively to the gold standard of pluripotency, the ESCs. The results ­provide great promise that gPSCs can be of importance for pra…

Homeobox protein NANOG0303 health sciencesTetraploid complementation assay030302 biochemistry & molecular biologyEmbryoid bodyBiologyEmbryonic stem cell3. Good healthCell biology03 medical and health sciencesStem cellInduced pluripotent stem cellReprogramming030304 developmental biologyAdult stem cell
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Nouvelles perspectives concernant la structure et la fonction du domaine carboxyl terminal de Hfq

2015

Accumulating evidence indicates that RNA metabolism components assemble into supramolecular cellular structures to mediate functional compartmentalization within the cytoplasmic membrane of the bacterial cell. This cellular compartmentalization could play important roles in the processes of RNA degradation and maturation. These components include Hfq, the RNA chaperone protein, which is involved in the post-transcriptional control of protein synthesis mainly by the virtue of its interactions with several small regulatory ncRNAs (sRNA). The Escherichia coli Hfq is structurally organized into two domains. An N-terminal domain that folds as strongly bent β-sheets within individual protomers to…

IDP intrinsically-disordered proteinslcsh:Lifelcsh:QR1-502sub-membrane macromolecular assemblyPlasma protein bindingsRNA small non-coding RNABiochemistrylcsh:Microbiologyamyloid fibrilsProtein biosynthesis0303 health sciences[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]Escherichia coli Proteins030302 biochemistry & molecular biologyHfqCTRp Hfq C-terminal peptideFTIR Fourier transform infrared spectroscopyNTR N-terminal regionCompartmentalization (psychology)Cell biology[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsRNA Bacterialsmall non-coding ribonucleic acid (RNA)BiochemistryFSD Fourier self-deconvolutionTransfer RNAAmyloid fibrilProtein BindingBiophysicsBiologyHost Factor 1 Protein03 medical and health sciencesEscherichia coliThT thioflavin T[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyProtein Structure QuaternaryncRNA regulatory non-coding RNAPost-transcriptional regulationMolecular Biology030304 developmental biologyOriginal PaperC-terminusRNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyCell Biologycellular compartmentalizationWT wild-typeProtein Structure Tertiarylcsh:QH501-531Host Factor 1 ProteinCTR Hfq C-terminal regionribonucleic acid (RNA) processing and degradationBiophysicpost-transcriptional regulationBioscience Reports
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ISWI Regulates Higher-Order Chromatin Structure and Histone H1 Assembly In Vivo

2007

Imitation SWI (ISWI) and other ATP-dependent chromatin-remodeling factors play key roles in transcription and other processes by altering the structure and positioning of nucleosomes. Recent studies have also implicated ISWI in the regulation of higher-order chromatin structure, but its role in this process remains poorly understood. To clarify the role of ISWI in vivo, we examined defects in chromosome structure and gene expression resulting from the loss of Iswi function in Drosophila. Consistent with a broad role in transcriptional regulation, the expression of a large number of genes is altered in Iswi mutant larvae. The expression of a dominant-negative form of ISWI leads to dramatic a…

Imitation SWINucleosome assemblyTranscription GeneticQH301-705.5RNA-POLYMERASE-IIPROTEINCHROMOSOME ARCHITECTUREGeneral Biochemistry Genetics and Molecular BiologyHistones03 medical and health sciencesNUCLEOSOME REMODELING FACTORHigher Order Chromatin StructureHistone H1NucleosomeAnimalsTRANSCRIPTIONBiology (General)LIVING CELLSMolecular Biology030304 developmental biologyGENE-EXPRESSIONRegulation of gene expressionGeneticsAdenosine Triphosphatases0303 health sciencesGeneral Immunology and MicrobiologybiologyGeneral Neuroscience030302 biochemistry & molecular biologyGenetics and GenomicsCell BiologyChromatin Assembly and DisassemblyChromatinChromatinCell biologyDROSOPHILAHistoneGene Expression RegulationLarvaMutationbiology.proteinLINKER HISTONEGeneral Agricultural and Biological SciencesResearch ArticleDevelopmental BiologyTranscription FactorsDOSAGE COMPENSATION
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The insect nephrocyte is a podocyte-like cell with a filtration slit diaphragm.

2008

The nephron is the basic structural and functional unit of the vertebrate kidney. It is composed of a glomerulus, the site of ultrafiltration, and a renal tubule, along which the filtrate is modified. Although widely regarded as a vertebrate adaptation, 'nephron-like' features can be found in the excretory systems of many invertebrates, raising the possibility that components of the vertebrate excretory system were inherited from their invertebrate ancestors. Here we show that the insect nephrocyte has remarkable anatomical, molecular and functional similarity to the glomerular podocyte, a cell in the vertebrate kidney that forms the main size-selective barrier as blood is ultrafiltered to …

ImmunoglobulinsMuscle ProteinsNephronBiologyGlomerulus (kidney)urologic and male genital diseasesArticlePodocyteCell LineNephrin03 medical and health sciencesmedicineAnimalsDrosophila Proteins030304 developmental biologyNEPH10303 health sciencesMultidisciplinaryurogenital systemPodocytes030302 biochemistry & molecular biologyMembrane ProteinsAnatomyFiltration diaphragmCell biologymedicine.anatomical_structureDrosophila melanogasterNephrocyte diaphragmnephrocytePodocinbiology.proteinSlit diaphragm
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