The Role of zinc in the disulphide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor.
about
Exploiting thiol modificationsBacterial Sigma Factors and Anti-Sigma Factors: Structure, Function and DistributionStructural and Biochemical Bases for the Redox Sensitivity of Mycobacterium tuberculosis RslARedox-dependent disulfide bond formation in SAP30L corepressor protein: Implications for structure and functionThe Mycobacterium tuberculosis extracytoplasmic-function sigma factor SigL regulates polyketide synthases and secreted or membrane proteins and is required for virulenceThe YjbH protein of Bacillus subtilis enhances ClpXP-catalyzed proteolysis of SpxThe RNA polymerase-binding protein RbpA confers basal levels of rifampicin resistance on Streptomyces coelicolorInvolvement of SigT and RstA in the differentiation of Streptomyces coelicolorMycothiol regulates and is regulated by a thiol-specific antisigma factor RsrA and sigma(R) in Streptomyces coelicolorSimultaneous Activation of Iron- and Thiol-Based Sensor-Regulator Systems by Redox-Active CompoundsZinc-responsive regulation of alternative ribosomal protein genes in Streptomyces coelicolor involves zur and sigmaR.Protection against electrophile and oxidant stress by induction of the phase 2 response: fate of cysteines of the Keap1 sensor modified by inducersRedox-Active Sensing by Bacterial DksA Transcription Factors Is Determined by Cysteine and Zinc ContentIdentification of a novel anti-sigmaE factor in Neisseria meningitidis.The 4-cysteine zinc-finger motif of the RNA polymerase regulator DksA serves as a thiol switch for sensing oxidative and nitrosative stress.Thiol-based redox switches and gene regulationFRET-based system for probing protein-protein interactions between σR and RsrA from Streptomyces coelicolor in response to the redox environmentDeterminants of redox sensitivity in RsrA, a zinc-containing anti-sigma factor for regulating thiol oxidative stress response.Structural characterization of the late competence protein ComFB from Bacillus subtilis.Evidence of a bacterial receptor for lysozyme: binding of lysozyme to the anti-σ factor RsiV controls activation of the ecf σ factor σV.The zinc-responsive regulator Zur controls a zinc uptake system and some ribosomal proteins in Streptomyces coelicolor A3(2).Bacterial redox sensors.Conservation of thiol-oxidative stress responses regulated by SigR orthologues in actinomycetes.The Anti-sigma Factor RsiV Is a Bacterial Receptor for Lysozyme: Co-crystal Structure Determination and Demonstration That Binding of Lysozyme to RsiV Is Required for σV ActivationRedox active thiol sensors of oxidative and nitrosative stress.Structural insights into the regulation of Bacillus subtilis SigW activity by anti-sigma RsiWCritical role of a single position in the -35 element for promoter recognition by Mycobacterium tuberculosis SigE and SigH.The extracytoplasmic function sigma factor EcfO protects Bacteroides fragilis against oxidative stress.Regulation of bacterial RNA polymerase sigma factor activity: a structural perspective.Regulation of the SigH stress response regulon by an essential protein kinase in Mycobacterium tuberculosis.Induction of a stable sigma factor SigR by translation-inhibiting antibiotics confers resistance to antibiotics.Insights into redox sensing metalloproteins in Mycobacterium tuberculosis.ROS-Mediated Signalling in Bacteria: Zinc-Containing Cys-X-X-Cys Redox Centres and Iron-Based Oxidative Stress.Conferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions.OsdR of Streptomyces coelicolor and the Dormancy Regulator DevR of Mycobacterium tuberculosis Control Overlapping Regulons.Environmental Sensing in Actinobacteria: a Comprehensive Survey on the Signaling Capacity of This Phylum.Zinc can play chaperone-like and inhibitor roles during import of mitochondrial small Tim proteins.Translational Control of the SigR-Directed Oxidative Stress Response in Streptomyces via IF3-Mediated Repression of a Noncanonical GTC Start Codon.Features of Rhodobacter sphaeroides ChrR required for stimuli to promote the dissociation of σ(E)/ChrR complexes.The anti-sigma factor RsrA responds to oxidative stress by reburying its hydrophobic core
P2860
Q24793687-121EAF7F-751C-4F23-A692-A6B8F220BCF1Q27012703-F1B8C178-8972-47C2-808C-7B4B7F3CFA99Q27660054-136D5BA3-C0D2-4F89-8165-0702232B1880Q28114970-5908C466-25A5-4A55-8CDB-CFA0809A1DB4Q28487267-DE12EAC1-5E38-4345-A899-B18A9090047EQ28488899-17B38B21-DEC3-4054-B699-E0A4C2D002DAQ28504062-4D939321-8F19-4DC3-B41F-D13F4DFDBA3AQ28504064-03931DF3-5385-4DBA-8720-DF966C801341Q28504071-1477DB58-3CA5-420B-89BF-5997F13AADBEQ28817677-AE029C29-0837-473F-975E-567ECD200680Q29347204-85F8E90E-28D1-41FB-B280-8FCD32E6FFBBQ29616503-745A6FC4-FD63-4843-AEC9-7C8B4141AF85Q30387100-A6A9B28F-DE2D-4177-B815-1E26D537651AQ33595238-76262EAB-608B-423E-8E4A-78D1C2CC04E4Q33739903-2B61576F-BDCA-40EB-B1E3-07ED8F85CDE8Q35040525-764FF758-52A9-4DE8-B3FD-57CF40E427B7Q35126579-362B68B9-C097-4C58-98E4-C9109468A520Q35224408-D7E0398C-9B3F-4B71-B519-524C6F8B3C61Q35237589-068EE836-75A9-4A64-9140-6C83C1FA2690Q35295202-B1345771-322F-4422-8A54-28AAA4B22671Q35879310-301F3BED-B00E-4D1C-925B-2D87133A345DQ35954265-7C619CE2-9BEC-463E-9FE7-182D5C4DDCAFQ35987220-08C8BB5D-90DC-4970-80D5-BC3D998B3F26Q36125077-6B62B0BF-6FB6-4096-8B33-2142F5D2A559Q36198016-059532F8-FC3B-4F56-8370-1CB564618238Q36314674-FA312E50-5182-46D9-9964-8CE24B809F76Q36483772-1C211A2A-7B1E-455B-8F5F-98086645B8EEQ36506198-1446C308-1314-41BF-A5DF-656E47874DCCQ36662639-C085BE00-58ED-4DD1-AAC9-D64B1426AFA2Q36861908-9F3A9B2F-A1DC-45E5-B9C5-9B36020FF8F8Q37040064-D781EAEA-C881-4641-A062-A42B21271A77Q37647932-341DDDA5-A7FA-47DF-8E2D-9A285D940D4CQ37942909-0EEFA106-84D2-4AFC-9190-6C4DDCEE3118Q38634845-8443EACA-9DD2-4E80-9E90-5F074C9FBBD7Q39206378-212C9DFC-8D39-4D58-BBB0-2E9655149269Q40926419-E7557EDD-C6FC-4267-B24E-8BC71048D83CQ41809788-7422D4E7-6CD4-40A3-AB53-44CD2F359186Q41976458-E4D13D9E-A6C4-4346-969B-092F476CAB25Q42152705-AE9FB6C1-A859-4A7B-A501-DD9D98CB9E86Q42405417-679FACCA-9EF5-42FD-96C7-7CF5FF690AF5
P2860
The Role of zinc in the disulphide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
The Role of zinc in the disulp ...... from Streptomyces coelicolor.
@en
The Role of zinc in the disulp ...... from Streptomyces coelicolor.
@nl
type
label
The Role of zinc in the disulp ...... from Streptomyces coelicolor.
@en
The Role of zinc in the disulp ...... from Streptomyces coelicolor.
@nl
prefLabel
The Role of zinc in the disulp ...... from Streptomyces coelicolor.
@en
The Role of zinc in the disulp ...... from Streptomyces coelicolor.
@nl
P50
P1476
The Role of zinc in the disulp ...... A from Streptomyces coelicolor
@en
P2093
Colin Kleanthous
Maureen J Bibb
P304
P356
10.1016/J.JMB.2003.08.038
P407
P577
2003-10-01T00:00:00Z