phoB Antibody

1. The results point to a model showing that PhoB is a component in the signal cascade regulating biofilm formation triggered by fluctuations of Polyphosphate levels in E. coli cells during stationary phase. PMID: 27023099
2. The expression timing of the core set of PhoB-regulated genes correlates well with the binding affinity of phosphorylated PhoB~P to individual promoters. PMID: 26015501
3. a combination of single-molecule and ensemble methods was used to investigate the binding mechanism and the impact of dimerization on the protein-DNA complex stability of PhoB(DBD) PMID: 24199636
4. Data indicate that dimerization constants for the PhoB heterodimer and homodimer (two phosphorylated monomers) were similar, but the rate constant for heterodimer phosphorylation was ~10-fold higher than for the monomer. PMID: 23760278
5. sigma(4) domain of RpoD achieves promoter recognition through the N-terminal portion of its DNA recognition helix. Unexpectedly, the same recognition helix contacts the transactivation loop and helices alpha2 and alpha3 of PhoB. PMID: 21829166
6. Crystallography and solution NMR data for the receiver domain of PhoB which show distinct 2-fold symmetric dimers in the inactive and active states. PMID: 16154092
7. analysis of cofactor-induced pre-active conformation in PhoB PMID: 16929106
8. PhoB has a role as a global regulator in Escherichia coli gene expression. PMID: 17020555
9. phosphorylation promotes dimerization via the alpha 4-beta 5-alpha 5 face, which enhances DNA binding and thus the ability of PhoB to regulate transcription. PMID: 19371748

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KEGG: ecj:JW0389

STRING: 316385.ECDH10B_0355