about
Classification and evolutionary history of the single-strand annealing proteins, RecT, Redbeta, ERF and RAD52The metabolic enzyme ManA reveals a link between cell wall integrity and chromosome morphologyStructure of the N-Terminal Oligomerization Domain of DnaD Reveals a Unique Tetramerization Motif and Provides Insights into Scaffold FormationMechanism of staphylococcal multiresistance plasmid replication origin assembly by the RepA proteinThe cyanobacterial cell division factor Ftn6 contains an N-terminal DnaD-like domainControl of initiation of sporulation by replication initiation genes in Bacillus subtilis.DnaB proteolysis in vivo regulates oligomerization and its localization at oriC in Bacillus subtilis.DnaD protein of Bacillus subtilis interacts with DnaA, the initiator protein of replicationBiophysical characterization of DNA binding from single molecule force measurementsWhen simple sequence comparison fails: the cryptic case of the shared domains of the bacterial replication initiation proteins DnaB and DnaD.The Bacillus subtilis DnaD protein: a putative link between DNA remodeling and initiation of DNA replication.The DNA-remodelling activity of DnaD is the sum of oligomerization and DNA-binding activities on separate domainsBreaking the rules: bacteria that use several DNA polymerase IIIs.Helicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis.Sequence of plasmid pGT5 from the archaeon Pyrococcus abyssi: evidence for rolling-circle replication in a hyperthermophileCharacterization of Lactococcus lactis UV-sensitive mutants obtained by ISS1 transposition.Characterization of Staphylococcus aureus Primosomal DnaD Protein: Highly Conserved C-Terminal Region Is Crucial for ssDNA and PriA Helicase Binding but Not for DnaA Protein-Binding and Self-TetramerizationAutonomous Replication of the Conjugative Transposon Tn916.Chromosomal replication initiation machinery of low-G+C-content FirmicutesStaphylococcus aureus single-stranded DNA-binding protein SsbA can bind but cannot stimulate PriA helicase.Nutritional control of elongation of DNA replication by (p)ppGppMapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus.Control of Initiation of DNA Replication in Bacillus subtilis and Escherichia coli.Replication and control of circular bacterial plasmids.Restart of DNA replication in Gram-positive bacteria: functional characterisation of the Bacillus subtilis PriA initiator.DNA inversion on conjugative plasmid pVT745.Untwisting of the DNA helix stimulates the endonuclease activity of Bacillus subtilis Nth at AP sitesIdentification of a Single Strand Origin of Replication in the Integrative and Conjugative Element ICEBs1 of Bacillus subtilisOrdered association of helicase loader proteins with the Bacillus subtilis origin of replication in vivo.The Bacillus subtilis DnaD and DnaB proteins exhibit different DNA remodelling activities.Single-molecule atomic force spectroscopy reveals that DnaD forms scaffolds and enhances duplex melting.The primosomal protein DnaD inhibits cooperative DNA binding by the replication initiator DnaA in Bacillus subtilis.Primosomal proteins DnaD and DnaB are recruited to chromosomal regions bound by DnaA in Bacillus subtilisReplication of Staphylococcal Resistance Plasmids.Bacillus subtilis DNA polymerases, PolC and DnaE, are required for both leading and lagging strand synthesis in SPP1 origin-dependent DNA replication.Structural analyses of the bacterial primosomal protein DnaB reveal that it is a tetramer and forms a complex with a primosomal re-initiation protein.
P2860
Q24805465-00765354-1B79-44DE-8FBF-7F01F39CE82CQ27346325-2717C48B-ED30-4023-9137-66D0A5AEFB17Q27649564-94E00131-921E-4D4D-A685-3FEA989515E7Q27684327-E95FB116-B230-4274-9859-56FA0C45583BQ33495698-A0AAD6DA-D1B2-4E6C-ACBC-70AB68CD89CCQ33603433-2EADC846-F1B5-459C-BF9F-511F155E22F1Q33871082-56FA1AC9-3EA2-42F8-AB83-91E6270AEECBQ33935662-215B0B41-ADEF-4E91-B886-85FF548A3B00Q34091700-8F4DC551-9361-4F23-9165-B5B8772F0679Q34298065-BCF6A261-4EC2-463E-B967-8589C5149A7CQ34551468-0B123EDD-C247-463F-A315-14A0B345E0DEQ34558332-C54C2B7A-C2EC-4F8E-B977-D41672EDDF24Q34953383-496DC94B-39A6-49D1-A320-D231F5FDC897Q35130498-6FFDFA5E-EA2D-4B6F-912D-B1C506D99904Q35608034-C2835FFB-261C-4C10-8E46-22419FA1C5DDQ35626161-EC21C6B5-92F1-4650-AE07-FD30AC4D3E29Q36052744-ABA749CD-A845-466B-8C28-2C377485BCC8Q37425423-D7DA110E-E6E1-4EA2-BB28-01E5D8E59B5AQ38026487-512DF409-FB82-48BF-9851-E5A0A6D83251Q38287634-0E35857A-026C-427C-81DD-6AD376BCF0EDQ38303861-65DF5114-945B-4191-A42C-791CC60301C7Q38642649-78DEFF94-C125-4AAB-A922-0EAF91B4A5E8Q39079493-BCB2217A-F99C-412B-B3C9-FBE99054D832Q39523346-9281B8E3-1C44-469E-A569-928BFB57CFF0Q39538408-B5E18BBA-4B69-4B3E-BFF3-B75721357007Q39680520-3F35C2F0-F7A9-4360-A35A-3397A05538D1Q40395945-E18DEB24-EA9D-4B14-8B0E-EF84ADC48DE0Q41247891-FFACD881-3AF6-4C43-9000-05AB361CD857Q41471640-9CE3E15E-A06D-40EA-877B-048F2DB4D1D3Q41838777-C20D3263-CBE8-45A2-8322-60D22AF62FB6Q42091977-55E63634-20E0-43FD-85D4-5D5CB26A1E50Q42321823-629E526D-662F-4C8B-B788-97F7C3B1F4C5Q42572155-2378C577-3A3A-4A8E-9F2C-6369510640E8Q47108095-3990F4B6-C4F7-441B-A54F-ED4BE934F5D0Q47132325-87F4F5AF-9D40-4DB5-9AA4-B9A621CF6E7DQ47952998-DB51DB2E-E9D4-4AB0-B5CE-53BC4D0CC55E
P2860
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Primosome assembly site in Bacillus subtilis.
@en
type
label
Primosome assembly site in Bacillus subtilis.
@en
prefLabel
Primosome assembly site in Bacillus subtilis.
@en
P2093
P2860
P1433
P1476
Primosome assembly site in Bacillus subtilis.
@en
P2093
P2860
P304
P407
P577
1995-06-01T00:00:00Z