about
Allele specific synthetic lethality between priC and dnaAts alleles at the permissive temperature of 30 degrees C in E. coli K-12Loading and activation of DNA replicative helicases: the key step of initiation of DNA replicationStructure of the N-Terminal Oligomerization Domain of DnaD Reveals a Unique Tetramerization Motif and Provides Insights into Scaffold FormationA novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loaderPrimase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficileAn expanded view of bacterial DNA replication.The cyanobacterial cell division factor Ftn6 contains an N-terminal DnaD-like domainIntragenic and extragenic suppressors of temperature sensitive mutations in the replication initiation genes dnaD and dnaB of Bacillus subtilis.Rapid exchange of bound ADP on the Staphylococcus aureus replication initiation protein DnaA.DnaB proteolysis in vivo regulates oligomerization and its localization at oriC in Bacillus subtilis.Biophysical 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 domainsHelicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis.Whole-genome sequencing of Bacillus subtilis XF-1 reveals mechanisms for biological control and multiple beneficial properties in plants.Replication Restart after Replication-Transcription Conflicts Requires RecA in Bacillus subtilis.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-TetramerizationDNA repair and genome maintenance in Bacillus subtilis.Bacteriophage replication modules.The PriA replication restart protein blocks replicase access prior to helicase assembly and directs template specificity through its ATPase activity.Transcription of the toxin genes present within the Staphylococcal phage phiSa3ms is intimately linked with the phage's life cycle.Transcription leads to pervasive replisome instability in bacteria.Recruitment to stalled replication forks of the PriA DNA helicase and replisome-loading activities is essential for survival.Chromosomal replication initiation machinery of low-G+C-content FirmicutesStaphylococcus aureus single-stranded DNA-binding protein SsbA can bind but cannot stimulate PriA helicase.Co-directional replication-transcription conflicts lead to replication restart.Replication Restart in Bacteria.Restart of DNA replication in Gram-positive bacteria: functional characterisation of the Bacillus subtilis PriA initiator.Untwisting of the DNA helix stimulates the endonuclease activity of Bacillus subtilis Nth at AP sitesOrdered 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.Anticipating chromosomal replication fork arrest: SSB targets repair DNA helicases to active forks.Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis.Requirements for replication restart proteins during constitutive stable DNA replication in Escherichia coli K-12.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 subtilisThe Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA.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
Q24809640-E4167DE5-47A2-4E44-A879-F29C4796E211Q27009085-912E096A-DB4A-4172-84C4-C5E6A9F0E893Q27649564-0740F8A1-AC7E-4AF4-82CF-19410D24E82AQ27653990-7FDAEAF4-FA57-4C43-B35D-2ED66309C3E3Q28357054-B6641A4B-5645-41DB-B120-E46913A8AF87Q31076593-1C143EBE-A082-4BE9-93DB-7F3E77927DF4Q33495698-8D0A2578-2111-4360-964F-A9C33BE1FDC1Q33496723-3A1AB4AA-532C-4E70-A170-49B141C47A68Q33553501-27C3C7AA-9723-4628-ABD7-9C5F7EEF3E88Q33871082-6D79688C-A60C-4F0E-81E0-E7401C3531DBQ34091700-D99C77E6-9B82-473A-B64E-54F09E5536EFQ34298065-61CACE19-96C6-477E-9E9F-5438F5D2E276Q34551468-0A2A4046-B362-4A65-B4CF-AE9E643BFBD9Q34558332-BE7AABEE-E88E-4C85-84F9-5F82404CE067Q35130498-6AD65968-FE2E-4769-994F-211C2DCA43A1Q35599000-26BA4FA3-3473-46D6-B94A-FF6E5A5A6338Q35914188-20B21DEC-BD0F-4147-833D-D89DA7122736Q36052744-13E1F80C-A04B-4A2B-9B4C-43272AE275F2Q36194928-532F9DA9-07D4-4B2C-BD2A-2F0489887C15Q36440552-0BDA4035-F7CC-494B-B8A5-9D99A6EDF7FCQ36596201-BF5B1829-7F5B-4626-B5F4-6531F5389C5CQ37062747-98B79DED-8FE5-4747-B586-61241B8E36DDQ37638992-6D244A7B-CD53-42BB-A5DD-0BC6E37F9C93Q37680371-631DEB2C-2A88-463C-A53A-98E4CCACE18AQ38026487-239E19EF-DC06-4954-9F96-FFE04ABAF33CQ38287634-3437FF77-B273-46BC-90D7-95E054BE392BQ38337096-275EB874-0916-494A-BDD3-62EFD67F14E1Q39188771-58933FDC-40CD-4EA5-9CB6-1402F8F5F0B3Q39538408-9FD3F124-2863-4EBB-B1BA-ADE83C94FAA2Q40395945-F72E08BC-7F57-4E06-A01C-83A03157B9C7Q41471640-B80C7348-4CD0-497D-B9AE-FFF218DA290DQ41838777-5B076E63-FAF5-4CF9-B842-BF3F7B3230CBQ41891443-DDFA4F96-784F-4FE1-999F-659EF51DFAABQ41907255-0908B7A1-922B-401D-AC71-58B482666AA3Q42012393-EDB02DE7-88FE-46CC-A781-52875CA7F9CDQ42091977-1E95FEE0-A0EA-4330-A47D-EEDB7173AFA8Q42321823-547CD546-CC74-4C02-A44C-23AAEFF99768Q42572155-C01D6FF6-535E-48EB-AB9A-2D30E5D78358Q42577246-77DE5310-EACD-4F96-B8B3-137A6BB62C21Q47952998-5746BFD6-7143-4A35-A1C5-999D27732910
P2860
description
2001 nî lūn-bûn
@nan
2001 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Early steps of Bacillus subtilis primosome assembly.
@ast
Early steps of Bacillus subtilis primosome assembly.
@en
Early steps of Bacillus subtilis primosome assembly.
@nl
type
label
Early steps of Bacillus subtilis primosome assembly.
@ast
Early steps of Bacillus subtilis primosome assembly.
@en
Early steps of Bacillus subtilis primosome assembly.
@nl
prefLabel
Early steps of Bacillus subtilis primosome assembly.
@ast
Early steps of Bacillus subtilis primosome assembly.
@en
Early steps of Bacillus subtilis primosome assembly.
@nl
P2093
P2860
P356
P1476
Early steps of Bacillus subtilis primosome assembly
@en
P2093
P2860
P304
45818-45825
P356
10.1074/JBC.M101996200
P407
P577
2001-12-01T00:00:00Z