CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY.
about
Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic StressStructural, kinetic and proteomic characterization of acetyl phosphate-dependent bacterial protein acetylationNε-lysine acetylation of a bacterial transcription factor inhibits Its DNA-binding activityBacterial protein acetylation: the dawning of a new age.Biologically active isoforms of CobB sirtuin deacetylase in Salmonella enterica and Erwinia amylovora.Acetylome analysis reveals diverse functions of lysine acetylation in Mycobacterium tuberculosis.Control of protein function by reversible Nɛ-lysine acetylation in bacteriaThe E. coli sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sitesCheY's acetylation sites responsible for generating clockwise flagellar rotation in Escherichia coliPost-translational modification of RNase R is regulated by stress-dependent reduction in the acetylating enzyme Pka (YfiQ).Glycolysis for Microbiome Generation.Essential Genes Embody Increased Mutational Robustness to Compensate for the Lack of Backup Genetic Redundancy.Sirtuin regulation in aging and injuryReversible acetylation on Lys501 regulates the activity of RNase IIReversible lysine acetylation is involved in DNA replication initiation by regulating activities of initiator DnaA in Escherichia coli.Sirtuin mechanism and inhibition: explored with N(ε)-acetyl-lysine analogs.Protein acetylation in archaea, bacteria, and eukaryotesProtein acetylation in prokaryotes.Protein acetylation affects acetate metabolism, motility and acid stress response in Escherichia coliBacterial protein acetylation: new discoveries unanswered questions.Regulation, Function, and Detection of Protein Acetylation in Bacteria.Lysine acetylation regulates the activity of Escherichia coli pyridoxine 5'-phosphate oxidase.A SIRT4-like auto ADP-ribosyltransferase is essential for the environmental growth of Mycobacterium smegmatis.Lysine acetylation regulates the activity of Escherichia coli S-adenosylmethionine synthase.Deacetylation of topoisomerase I is an important physiological function of E. coli CobB.Protein acetylation in prokaryotes increases stress resistance.Alternate deacylating specificities of the archaeal sirtuins Sir2Af1 and Sir2Af2.Reversibly acetylated lysine residues play important roles in the enzymatic activity of Escherichia coli N-hydroxyarylamine O-acetyltransferase.Protein acetylation: an important mechanism in actinobacteria.Lysine acetylation regulates the function of the global anaerobic transcription factor FnrL in Rhodobacter sphaeroides.CheY acetylation is required for ordinary adaptation time in Escherichia coli chemotaxis.Studying the Lysine Acetylation of Malate Dehydrogenase.Global identification of CobB interactors by an Escherichia coli proteome microarray.Accurate Quantification of Site-specific Acetylation Stoichiometry Reveals the Impact of Sirtuin Deacetylase CobB on the E. coli Acetylome.Protein acetylation and butyrylation regulate the phenotype and metabolic shifts of the endospore-forming Clostridium acetobutylicum.Protein Acetylation Mediated by YfiQ and CobB Is Involved in the Virulence and Stress Response of Yersinia pestis.Prokaryotic Nε-lysine acetylomes and implications for new antibiotics.Acetylation of lysine 182 inhibits the ability of Mycobacterium tuberculosis DosR to bind DNA and regulate gene expression during hypoxia.Bacterial moving and shaking: the 11th blast meeting
P2860
Q26801091-D364589E-D99C-440A-A167-C322A89592ADQ27683517-63666536-0E13-47B2-B986-372B61663E3DQ28476671-8B511E8F-9A94-4836-96D5-F49F722B3CE7Q34009079-63E07D6B-B6CE-4BD4-9D20-456399734B78Q34309358-3AED2F45-D8EC-40C6-A359-6AED2DB722EBQ34634921-5DEABD11-F5A0-4639-A5FA-B1C15FA355BCQ34809835-CAAAD10C-5D0D-484E-9DFB-91615ED5DC7EQ35106207-E3408653-1020-4EDA-8A28-1EDC334CEDC5Q35591644-53722508-A9B9-47E6-A4F1-A47B20C7DA9DQ35682203-03BC0EE0-DBF2-466C-B84C-9A25042E5A1EQ35694201-5B04250C-8E54-4344-AF6B-17F22455066AQ36229579-2384D16D-DB9C-4C01-B15A-12BCFE4369A6Q36379286-A8DC710B-B3A4-491D-A1BB-80F39166756CQ36701131-6E95B2D3-6C31-4374-A840-3A5C396CE997Q37147957-71778695-D9B9-448B-9D91-AB6484D55649Q37788970-9503F81F-F87A-4BAB-A547-3C47BB02C925Q37795592-23A94765-889E-4936-8BFA-C62004B7FEF9Q37889858-09CD345C-A015-4DA9-BEAA-A13DB6599D0AQ38302162-4F5F45EA-0127-41A6-B793-8D5CAFC79DCDQ38667629-DC12B178-382A-4843-B2DA-AC46EF9A5A58Q38691364-67647D56-C629-427F-9AF8-F0F9DEFB22CAQ39049184-82219ED8-0EAE-4798-8440-4CE4918A6F5CQ40191162-0EA444DB-4EB1-4FFA-8DA5-96DA1C1FF313Q40649176-B8B3E993-1EDA-4EC1-8CC7-4FF09B832692Q41693951-FDC5A382-FD52-48E0-B7C1-19AC5E66737FQ41811914-DC3F5346-D503-4D73-AE7A-20D5E05DD5BFQ41827709-315AA1B9-3B07-460E-BE5F-708C15AE82AAQ45376320-C09D4625-B0DB-4238-BB80-39C3FFE442E6Q47558014-15140150-7657-40C0-8D56-E7E946085502Q48316779-0AEF973C-68E1-4DC1-993D-7C3F09AE9687Q50623973-F669DC21-23BD-4D73-AE03-88CB1DFCA6FFQ50664922-8B158766-C360-456A-8C95-D15E556457D2Q51076279-3896F4BC-1643-4C7F-A6DA-D063E9857C85Q51114432-6BAECAF0-855E-40BD-868C-0F911E9CE945Q52727532-354C27D1-1395-4B93-82BC-AC09BEDF8C1CQ53699174-183B1BE1-A12E-4312-AACE-BDFC4EDE4E6DQ54332700-028EA1A3-F573-447F-BB2F-05A508982EEEQ55174955-DA174E78-103A-4E92-955D-2D8FE68A900DQ58072592-12CD7E03-1C9A-49AC-B7A0-6041623BEB1F
P2860
CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY.
@en
type
label
CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY.
@en
prefLabel
CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY.
@en
P2093
P2860
P1476
CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY.
@en
P2093
Chuan-Le Xiao
Hong-Ping Wei
Jiao-Yu Deng
Li-Wei Wang
Xian-En Zhang
Xu-De Wang
Yuan-Yuan Chen
P2860
P304
P356
10.1111/J.1365-2958.2010.07125.X
P407
P577
2010-03-16T00:00:00Z