The major cold shock protein of Bacillus subtilis CspB binds with high affinity to the ATTGG- and CCAAT sequences in single stranded oligonucleotides.
about
Cold shock domain proteins repress transcription from the GM-CSF promoterMassive presence of the Escherichia coli 'major cold-shock protein' CspA under non-stress conditions.Single-stranded DNA-binding proteins: multiple domains for multiple functionsCommon mode of DNA binding to cold shock domains. Crystal structure of hexathymidine bound to the domain-swapped form of a major cold shock protein from Bacillus caldolyticusCrystallization and X-ray structure of cold-shock protein E fromSalmonella typhimuriumSolution structure of the single-stranded DNA binding protein of the filamentous Pseudomonas phage Pf3: similarity to other proteins binding to single-stranded nucleic acidsCrystal structure of CspA, the major cold shock protein of Escherichia coliSpecific polar localization of ribosomes in Bacillus subtilis depends on active transcriptionCold shock stress-induced proteins in Bacillus subtilisExtremely rapid protein folding in the absence of intermediates.Pathogenic Yersinia species carry a novel, cold-inducible major cold shock protein tandem gene duplication producing both bicistronic and monocistronic mRNA.Influence of the stability of a fused protein and its distance to the amyloidogenic segment on fibril formation.Altered growth, pigmentation, and antimicrobial susceptibility properties of Staphylococcus aureus due to loss of the major cold shock gene cspB.AT-rich region and repeated sequences - the essential elements of replication origins of bacterial replicons.Coping with the cold: the cold shock response in the Gram-positive soil bacterium Bacillus subtilis.The cold shock response of the psychrotrophic bacterium Pseudomonas fragi involves four low-molecular-mass nucleic acid-binding proteins.Purification and Characterization of a Novel Cold Shock Protein-Like Bacteriocin Synthesized by Bacillus thuringiensis.Mutational analysis of the putative nucleic acid-binding surface of the cold-shock domain, CspB, revealed an essential role of aromatic and basic residues in binding of single-stranded DNA containing the Y-box motif.Binding of Y-box proteins to RNA: involvement of different protein domainsSequence specificity of single-stranded DNA-binding proteins: a novel DNA microarray approachInteractions of the cold shock protein CspB from Bacillus subtilis with single-stranded DNA. Importance of the T base content and position within the template.Interactions of the major cold shock protein of Bacillus subtilis CspB with single-stranded DNA templates of different base composition.The family of cold shock proteins of Bacillus subtilis. Stability and dynamics in vitro and in vivo.Identification and purification of a family of dimeric major cold shock protein homologs from the psychrotrophic Bacillus cereus WSBC 10201.A folded and functional protein domain in an amyloid-like fibril.Complementation of cold shock proteins by translation initiation factor IF1 in vivo.Genomewide transcriptional analysis of the cold shock response in Bacillus subtilis.Cloning and characterization of cspL and cspP, two cold-inducible genes from Lactobacillus plantarum.CspA regulates pigment production in Staphylococcus aureus through a SigB-dependent mechanism.Growth-dependent activity of the cold shock cspA promoter + 5' UTR and production of the protein CspA in Staphylococcus aureus Newman.Functional Activation of the Flagellar Type III Secretion Export ApparatusSingle-stranded DNA binding of the cold-shock protein CspB from Bacillus subtilis: NMR mapping and mutational characterization.Heat stable ssDNA/RNA-binding activity of a wheat cold shock domain protein.Different morphology of amyloid fibrils originating from agitated and non-agitated conditions
P2860
Q24313094-771187AF-52B6-41C6-A1F5-C79414FE81B4Q24534011-93C44FA6-55DF-4396-9DEE-B999E6BD7E5EQ27027869-E8E887A7-03B0-4F02-B8AA-F8A6838105F7Q27643708-4854EB64-C4E9-4023-BBCA-CF1BB6490260Q27646708-2257FE27-4156-4BF8-8553-6B3BE35179BFQ27729479-39D7CB80-F640-4951-93FF-2989279EB2DDQ27731411-4251E3B2-45AD-4E7F-A6FD-FAA810E03FE8Q28344590-115D44DF-10CF-4D28-87CD-7C3DAA8D19BEQ28488921-3F7FD7FE-FF50-4EEA-8B4A-B474B861DF08Q30193236-51E2F06E-5D2E-4A67-B5E6-9FB1A93FFB8EQ30788563-32D13AB7-0A61-47E1-A9DA-32368A427169Q33760952-C596478B-FAB9-469A-BE89-DC2CB9C1608BQ33876570-85ECA3C2-73CA-4684-9941-D57B7E9CB5B3Q34233413-3D6A5021-AB9B-457A-9DD7-E5CB4D88D480Q34780391-ECD4B27E-F8F2-431A-84EA-90504872CE5BQ35633018-5DB47148-C4C9-4D8E-A460-C56F41FD1D94Q37352800-DF6CD0CB-925A-42DB-AA1D-542EFC7C3BC7Q38296241-FC545C38-15B2-4E9C-9ACE-F862998AD3FCQ38301037-047689FE-3C77-4E73-9EE8-06B6B3C27D12Q38301921-CB85741B-3E83-4315-A9BC-09E02204770BQ38302626-88978801-8D94-4C47-9566-25B826D32A5EQ38318501-7FB98B94-C044-4EF2-BD25-C46ED51C8997Q38329012-6F2D71E3-8961-47C6-8E9D-9B0DD4E934E5Q38358432-D022DC04-1D22-48B5-85E6-598DFEF140FAQ38528901-B2CF1961-D0AC-47A7-BA17-462C588465D5Q39505696-082B10BD-B48E-4BCA-AA49-034AD46CD6F4Q39741356-0A4C0235-C57B-4A16-8ECB-2570B64D079BQ39845588-8A256D67-B068-46E9-AB16-93339EB27438Q39892023-8E096749-56AA-449A-8E77-F0042BB4C6B4Q41018467-15F7579C-102B-4634-A0C7-77A2A7D9AA2BQ42187679-AFE17A23-F27E-495C-AD45-4D50FD9DE98AQ43137278-541985ED-2EDF-475B-BF7A-581506AC8EA7Q46657873-880C42B5-59A6-457B-9DFF-6D7FBE48CEF1Q58125089-C24D7A79-8B40-47CB-B116-2AE7D0ECFB0D
P2860
The major cold shock protein of Bacillus subtilis CspB binds with high affinity to the ATTGG- and CCAAT sequences in single stranded oligonucleotides.
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
The major cold shock protein o ...... gle stranded oligonucleotides.
@en
type
label
The major cold shock protein o ...... gle stranded oligonucleotides.
@en
prefLabel
The major cold shock protein o ...... gle stranded oligonucleotides.
@en
P2860
P1433
P1476
The major cold shock protein o ...... gle stranded oligonucleotides.
@en
P2093
Graumann P
Marahiel MA
P2860
P304
P356
10.1016/0014-5793(94)80355-2
P407
P577
1994-01-01T00:00:00Z