Search results for "030302 biochemistry & molecular biology"

showing 10 items of 238 documents

RepeatsDB in 2021: improved data and extended classification for protein tandem repeat structures

2020

The RepeatsDB database (URL: https://repeatsdb.org/) provides annotations and classification for protein tandem repeat structures from the Protein Data Bank (PDB). Protein tandem repeats are ubiquitous in all branches of the tree of life. The accumulation of solved repeat structures provides new possibilities for classification and detection, but also increasing the need for annotation. Here we present RepeatsDB 3.0, which addresses these challenges and presents an extended classification scheme. The major conceptual change compared to the previous version is the hierarchical classification combining top levels based solely on structural similarity (Class > Topology > Fold) with two new lev…

Repetitive Sequences Amino AcidAcademicSubjects/SCI00010BiologíaStatistics as TopicProtein Data Bank (RCSB PDB)Computational biologyBiologyRepetitive SequencesGene Ontology; HEK293 Cells; HeLa Cells; Humans; Proteins; Reproducibility of Results; Statistics as Topic; User-Computer Interface; Databases Protein; Repetitive Sequences Amino Acid; Tandem Repeat SequencesDatabases03 medical and health sciencesAnnotationUser-Computer InterfaceProtein structureSimilarity (network science)Tandem repeatGeneticsDatabase IssueHumansDatabases ProteinCiencias Exactasdatabase030304 developmental biology0303 health sciencesHierarchy (mathematics)Protein030302 biochemistry & molecular biologyProteinsReproducibility of Resultscomputer.file_formatProtein Data BankClass (biology)proteinsAmino AcidComputingMethodologies_PATTERNRECOGNITIONGene OntologyHEK293 CellsclassificationTandem Repeat Sequencesprotein tandem repeat structures[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]computerHeLa CellsNucleic Acids Research
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Repeatability in protein sequences

2019

Low complexity regions (LCRs) in protein sequences have special properties that are very different from those of globular proteins. The rules that define secondary structure elements do not apply when the distribution of amino acids becomes biased. While there is a tendency towards structural disorder in LCRs, various examples, and particularly homorepeats of single amino acids, suggest that very short repeats could adopt structures very difficult to predict. These structures are possibly variable and dependant on the context of intra- or inter-molecular interactions. In general, short repeats in LCRs can induce structure. This could explain the observation that very short (non-perfect) rep…

Repetitive Sequences Amino AcidGlobular proteinSaccharomyces cerevisiaeContext (language use)Computational biologyProtein–protein interactionEvolution Molecular03 medical and health sciencesSequence Analysis ProteinStructural BiologyHumansArabidopsis thalianaAmino Acid SequenceDatabases ProteinProtein secondary structure030304 developmental biologychemistry.chemical_classification0303 health sciencesbiology030302 biochemistry & molecular biologyProteinsbiology.organism_classificationAmino acidchemistrySequence AlignmentAlgorithmsFunction (biology)Journal of Structural Biology
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Flanking regions determine the structure of the poly-glutamine homo- repeat in huntingtin through mechanisms common among glutamine-rich human protei…

2020

International audience; The causative agent of Huntington's disease, the poly-Q homo-repeat in the N-terminal region of huntingtin (httex1), is flanked by a 17-residue-long fragment (N17) and a proline-rich region (PRR), which promote and inhibit the aggregation propensity of the protein, respectively, by poorly understood mechanisms. Based on experimental data obtained from site-specifically labeled NMR samples, we derived an ensemble model of httex1 that identified both flanking regions as opposing poly-Q secondary structure promoters. While N17 triggers helicity through a promiscuous hydrogen bond network involving the side chains of the first glutamines in the poly-Q tract, the PRR prom…

Repetitive Sequences Amino AcidHuntingtinAmino Acid Motifs[SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biophysics03 medical and health sciencesHuntington's diseaseStructural BiologyHuman proteome projectmedicineHumans[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Molecular BiologyHuman proteinsProtein secondary structure[SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]030304 developmental biology[INFO.INFO-BI] Computer Science [cs]/Bioinformatics [q-bio.QM]Huntingtin Protein0303 health sciencesChemistry030302 biochemistry & molecular biologyPromotermedicine.diseaseCell biologyIntrinsically Disordered ProteinsGlutamine[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsPolyglutamic Acid[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]Low Complexity Region
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Interaction of the retinoic acid signaling pathway with spicule formation in the marine sponge Suberites domuncula through activation of bone morphog…

2011

Abstract Background The formation of the spicules in siliceous sponges involves the formation of cylinder-like structures in the extraspicular space, composed of the enzyme silicatein and the calcium-dependent lectin. Scope of review Molecular cloning of the cDNAs (carotene dioxygenase, retinal dehydrogenase, and BMB-1 [bone morphogenic protein-1]) from the demosponge Suberites domuncula was performed. These tools were used to understand the retinoid metabolism in the animal by qRT-PCR, immunoblotting and TEM. Major conclusions We demonstrate that silintaphin-2, a silicatein-interacting protein, is processed from a longer-sized 15-kDa precursor to a truncated, shorter-sized 13 kDa calcium-b…

Retinal dehydrogenaseMolecular Sequence DataBiophysicsRetinoic acidMarine BiologyTretinoinReal-Time Polymerase Chain ReactionBiochemistryBone morphogenetic protein 1Bone Morphogenetic Protein 103 medical and health scienceschemistry.chemical_compoundDemospongeSponge spiculeAnimalsCloning MolecularMolecular BiologyDNA Primers030304 developmental biology0303 health sciencesBase Sequencebiology030302 biochemistry & molecular biologybiology.organism_classificationPoriferaSuberites domunculaSpongechemistryBiochemistrySignal transductionSignal TransductionBiochim. Biophys. Acta
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The telomeric Cdc13-Stn1-Ten1 complex regulates RNA polymerase II transcription

2019

Advance article.

S phase transcribed genesTranscription GeneticChromosomal Proteins Non-HistoneCell Cycle ProteinsRNA polymerase IIBur1[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Genome Integrity Repair and ReplicationS Phase0302 clinical medicineTranscription (biology)Gene Expression Regulation FungalTranscriptional regulation0303 health sciencesCdc13-Stn1-Ten1biology030302 biochemistry & molecular biologyTranscription regulationRNA pol IIChromatinCyclin-Dependent KinasesCell biologyTelomeres030220 oncology & carcinogenesisRNA Polymerase IITranscriptional Elongation FactorsSaccharomyces cerevisiae ProteinsDNA polymerase IITelomere-Binding ProteinsSaccharomyces cerevisiae[SDV.CAN]Life Sciences [q-bio]/CancerSaccharomyces cerevisiaeCST complex03 medical and health sciencesGeneticsBudding yeastGenomesGene030304 developmental biologyHmo1RNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyPromoterbiology.organism_classificationCromosomesTelomerebiology.proteinSpt5Cyclin-Dependent Kinase-Activating Kinase
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Isolation of the silicatein-α interactor silintaphin-2 by a novel solid-phase pull-down assay.

2011

The skeleton of siliceous sponges consists of amorphous biogenous silica (biosilica). Biosilica formation is driven enzymatically by means of silicatein(s). During this unique process of enzymatic polycondensation, skeletal elements (spicules) that enfold a central proteinaceous structure (axial filament), mainly comprising silicatein, are formed. However, only the concerted action of silicatein and other proteins can explain the genetically controlled diversity of spicular morphotypes, from simple rods with pointed ends to intricate structures with up to six rays. With the scaffold protein silintaphin-1, a first silicatein interactor that facilitates the formation of the axial filament and…

Scaffold proteinSpiculeImmunoprecipitationMolecular Sequence DataNanotechnologyBiologyFlagellumBiochemistry03 medical and health sciencesSponge spiculePhase (matter)Two-Hybrid System TechniquesProtein Interaction MappingAnimalsInteractorAmino Acid Sequence030304 developmental biology0303 health sciences030302 biochemistry & molecular biologySilicon DioxideCathepsinsYeastProtein TransportSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationBiophysicsAutoradiographyCalciumSuberitesProtein BindingBiochemistry
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Functional roles of the membrane-associated AAV protein MAAP

2021

AbstractWith a limited coding capacity of 4.7 kb, adeno-associated virus (AAV) genome has evolved over-lapping genes to maximise the usage of its genome. An example is the recently found ORF in the cap gene, encoding membrane-associated accessory protein (MAAP), located in the same genomic region as the VP1/2 unique domain, but in a different reading frame. This 13 KDa protein, unique to the dependovirus genus, is not homologous to any known protein. Our studies confirm that MAAP translation initiates from the first CTG codon found in the VP1 ORF2. We have further observed MAAP localised in the plasma membrane, in the membranous structures in close proximity to the nucleus and to the nuclea…

SciencevirusesGenetic VectorsBiologyVirus ReplicationGenomeinfektiotArticleVirusViral Proteins03 medical and health scienceschemistry.chemical_compoundCapsidGene therapyPlasmidProtein sequencingHumansGeneparvovirukset030304 developmental biology0303 health sciencesMultidisciplinaryMolecular engineeringVirus Assembly030302 biochemistry & molecular biologyQVirionRMembrane ProteinsTranslation (biology)DependovirusCell biologyCapsidchemistryMedicineCapsid ProteinsproteiinitDNAPlasmidskapsidi
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PlaToLoCo: the first web meta-server for visualization and annotation of low complexity regions in proteins

2020

Abstract Low complexity regions (LCRs) in protein sequences are characterized by a less diverse amino acid composition compared to typically observed sequence diversity. Recent studies have shown that LCRs may co-occur with intrinsically disordered regions, are highly conserved in many organisms, and often play important roles in protein functions and in diseases. In previous decades, several methods have been developed to identify regions with LCRs or amino acid bias, but most of them as stand-alone applications and currently there is no web-based tool which allows users to explore LCRs in protein sequences with additional functional annotations. We aim to fill this gap by providing PlaToL…

Sequence analysisAcademicSubjects/SCI00010Protein domainComputational biologyBiologyDomain (software engineering)Computer graphics03 medical and health sciencesAnnotationProtein DomainsSequence Analysis ProteinGeneticsComputer GraphicsHumansAmino Acids030304 developmental biology0303 health sciencesIntersection (set theory)030302 biochemistry & molecular biologyMembrane ProteinsProteinsMolecular Sequence AnnotationVisualizationMolecular Sequence AnnotationWeb Server IssueSoftwareNucleic Acids Research
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Efficient DNA Packaging of Bacteriophage PRD1 Requires the Unique Vertex Protein P6

2007

ABSTRACT The assembly of bacteriophage PRD1 proceeds via formation of empty procapsids containing an internal lipid membrane, into which the linear double-stranded DNA genome is subsequently packaged. The packaging ATPase P9 and other putative packaging proteins have been shown to be located at a unique vertex of the PRD1 capsid. Here, we describe the isolation and characterization of a suppressor-sensitive PRD1 mutant deficient in the unique vertex protein P6. Protein P6 was found to be an essential part of the PRD1 packaging machinery; its absence leads to greatly reduced packaging efficiency. Lack of P6 was not found to affect particle assembly, because in the P6-deficient mutant infecti…

Specificity factorImmunologyMutantBiologymedicine.disease_causeMicrobiologyBacteriophageViral Proteins03 medical and health scienceschemistry.chemical_compoundVirologyDNA PackagingmedicineBacteriophage PRD1Lipid bilayer030304 developmental biology0303 health sciencesMutationStructure and AssemblyVirus Assembly030302 biochemistry & molecular biologyVirionTectivirusSalmonella entericabiology.organism_classificationMolecular biologychemistryCapsidInsect ScienceMutationBiophysicsDNAJournal of Virology
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Proteomic analysis of the acid-soluble nacre matrix of the bivalve Unio pictorum: detection of novel carbonic anhydrase and putative protease inhibit…

2010

10 pages; International audience; The matrix extracted from mollusc shell nacre is a mixture of proteins and glycoproteins that is thought to play a major role in controlling biomineral synthesis and in increasing its mechanical properties. We investigated the nacreous shell of the freshwater mussel Unio pictorum, to which we applied a proteomics approach adapted to mollusc shell proteins. On one hand, the acid-soluble nacre matrix was fractionated by SDS-PAGE and the five main protein bands (P95, P50, P29, P16, and P12) were digested with trypsin and analyzed by nanoLC-MS/MS followed by de novo sequencing. On the other hand, the acid-soluble nacre matrix was analyzed in a similar manner, w…

Spectrometry Mass Electrospray IonizationProteomeMolecular Sequence DataBioinformaticsProteomicsBiochemistryHomology (biology)03 medical and health sciencesUnioSequence Analysis ProteinCarbonic anhydraseMollusc shellmedicineAnimalsProtease InhibitorsAmino Acid SequenceDatabases Protein[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular BiologyCarbonic Anhydrases030304 developmental biologychemistry.chemical_classification0303 health sciencesExpressed sequence tagbiology030302 biochemistry & molecular biologyOrganic ChemistryUnio pictorumTrypsinbiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialschemistryBiochemistrybiology.proteinMolecular MedicineGlycoproteinChromatography Liquidmedicine.drug
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