Identification of residues in the Mu transposase essential for catalysis.
about
Three new structures of the core domain of HIV-1 integrase: an active site that binds magnesiumPIN domain of Nob1p is required for D-site cleavage in 20S pre-rRNAThe PINc domain protein Utp24, a putative nuclease, is required for the early cleavage steps in 18S rRNA maturation.Soluble expression, purification and characterization of the full length IS2 Transposase.Universal platform for quantitative analysis of DNA transposition.Arrayed transposase-binding sequences on the ends of transposon Tn5090/Tn402Mutational analysis of highly conserved aspartate residues essential to the catalytic core of the piggyBac transposaseSolution structure of the Mu end DNA-binding ibeta subdomain of phage Mu transposase: modular DNA recognition by two tethered domains.Transposase makes critical contacts with, and is stimulated by, single-stranded DNA at the P element termini in vitro.The same two monomers within a MuA tetramer provide the DDE domains for the strand cleavage and strand transfer steps of transposition.Detection of RAG protein-V(D)J recombination signal interactions near the site of DNA cleavage by UV cross-linking.Rag-1 mutations associated with B-cell-negative scid dissociate the nicking and transesterification steps of V(D)J recombination.Characterization of ISRgn1, a novel insertion sequence of the IS3 family isolated from a bacteriocin-negative mutant of Ruminococcus gnavus E1.Identification of four acidic amino acids that constitute the catalytic center of the RuvC Holliday junction resolvase.Flexibility in MuA transposase family protein structures: functional mapping with scanning mutagenesis and sequence alignment of protein homologues.Analysis of Tc1-Mariner elements in Sclerotinia sclerotiorum suggests recent activity and flexible transposases.Nicking is asynchronous and stimulated by synapsis in 12/23 rule-regulated V(D)J cleavage.Characteristics of MuA transposase-catalyzed processing of model transposon end DNA hairpin substrates.Presence of a characteristic D-D-E motif in IS1 transposase.The terminal nucleotide of the Mu genome controls catalysis of DNA strand transfer.Trans catalysis in Tn5 transposition.Organization and dynamics of the Mu transpososome: recombination by communication between two active sites.Mutational analysis of RAG1 and RAG2 identifies three catalytic amino acids in RAG1 critical for both cleavage steps of V(D)J recombination.Mutagenesis of the IS1 transposase: importance of a His-Arg-Tyr triad for activity.Multiple effects of mutations in human immunodeficiency virus type 1 integrase on viral replicationAssembly and catalytic properties of retrovirus integrase-DNA complexes capable of efficiently performing concerted integration.Mutational analysis of the adeno-associated virus Rep68 protein: identification of critical residues necessary for site-specific endonuclease activity.Mutations in the mariner transposase: the D,D(35)E consensus sequence is nonfunctionalThe mu transpososome through a topological lens.Dissecting the roles of MuB in Mu transposition: ATP regulation of DNA binding is not essential for target deliveryBacteriophage Mu integration in yeast and mammalian genomes.The phage Mu transpososome core: DNA requirements for assembly and function.A domain sharing model for active site assembly within the Mu A tetramer during transposition: the enhancer may specify domain contributions.The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition.Application of the bacteriophage Mu-driven system for the integration/amplification of target genes in the chromosomes of engineered Gram-negative bacteria--mini review.A model of the replication fork blocking protein Fob1p based on the catalytic core domain of retroviral integrasesPartial functional deficiency of E160D flap endonuclease-1 mutant in vitro and in vivo is due to defective cleavage of DNA substrates.Site-directed mutagenesis of conserved aspartates, glutamates and arginines in the active site region of Escherichia coli DNA topoisomerase I.Reorganization of the Mu transpososome active sites during a cooperative transition between DNA cleavage and joining.Mutations in nonconserved domains of Ty3 integrase affect multiple stages of the Ty3 life cycle
P2860
Q27764898-3C37605F-EEB8-4B21-B5AE-705AF4F43320Q27933019-FBCFB4DB-8DB6-40ED-8312-FA124E01E927Q27936907-29A516CC-3620-4202-B8B3-1423050E874AQ30408688-1A592311-63A6-4144-80B2-B9A1B757D810Q30497681-8446AB53-79A5-451E-8C8A-68774EBA21A5Q30978563-AF7BED4A-1720-41A3-BB1E-B425815FE8EFQ33359287-DF8AAE76-41A6-4F40-827F-5293474F8DF4Q33887936-69651A85-51FE-4331-B57B-8FDBCADDB4DAQ33888644-0DC0B8A9-B105-4505-A904-29AED2252E21Q33889071-004EED2C-D535-4586-AF7E-BDAF55F035FFQ33958242-440E485B-235C-4D2A-8AF2-7BB82BB1572FQ33968434-5FBD456C-F933-4C58-B84A-89D60E62A774Q34057717-A72A9DEA-00CD-48EF-B58D-461766A68542Q34058459-C69AF8EF-71C6-42B7-835D-2812A4EA445FQ34292691-0E9B55FA-07EE-4DB3-B94F-862C7DA608C6Q34302905-DEB9FB7D-56EC-4F20-B607-4424DDDF2385Q34641788-65387B94-6FA8-4A09-B747-86EC2C532A13Q34666794-5A14DC97-2D0D-4643-BB38-85CC9B89BE45Q34842642-7A4C2C77-53FB-491A-89C3-93A56DA641E5Q35145917-1C3E1417-0AD4-4CD0-9BDB-BE986BB8EC15Q35191790-07798863-CCE6-40CC-9239-C3D8C3B060A4Q35208441-5AF9BC01-BEFE-4CD9-9627-B673D81AD70EQ35210006-265D11EC-57CA-408A-9CAE-73C7F99AC625Q35593721-11C258CB-0FAA-4B4F-951A-34B44468C94BQ35838477-339BE1FA-1FDF-453E-9B8A-293112E10016Q35851776-0CD84BB4-55B1-49A4-8E6B-F7A08BA7FE45Q35880448-E75D2EF9-EF1F-4665-8427-2826CEAC4C0BQ35995628-39513CE1-66A7-4A07-972D-C600F4B69582Q36648418-445E892A-0B59-44AD-9371-51B00CB4CA76Q36858379-5129ACFF-408B-41EA-84D8-D7071E32415BQ37014688-3379819E-BA2D-487F-8B9A-849EE3B8FC67Q37623561-4BB55E7C-8116-4DB2-A36B-0179A3EABAECQ37697577-15AB2C33-0677-4D97-B09A-A5B5AB87EE21Q37732174-7819F242-2B84-4EA4-821D-3A8394614544Q37893526-6283760C-FB91-4228-808B-D3804421AB68Q38269549-A2E0BD8A-8444-42E6-A6F7-E8A114D074D1Q38330972-CB9CBBC6-CBCF-42BE-A9F4-33001EF1EC8CQ38337782-2D6DB134-237D-4258-97CC-8FD4C643D5B6Q38348560-4C6A0F33-BA90-45A1-A9D9-393A4EA6B8AAQ39548812-46DA3AF2-4030-4F9B-912B-4EA312B6B042
P2860
Identification of residues in the Mu transposase essential for catalysis.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Identification of residues in the Mu transposase essential for catalysis.
@ast
Identification of residues in the Mu transposase essential for catalysis.
@en
type
label
Identification of residues in the Mu transposase essential for catalysis.
@ast
Identification of residues in the Mu transposase essential for catalysis.
@en
prefLabel
Identification of residues in the Mu transposase essential for catalysis.
@ast
Identification of residues in the Mu transposase essential for catalysis.
@en
P2860
P356
P1476
Identification of residues in the Mu transposase essential for catalysis.
@en
P2860
P304
P356
10.1073/PNAS.91.14.6654
P407
P577
1994-07-01T00:00:00Z