rfaH Antibody

1. The presence of the leucine-rich element in the RfaH C-terminal domain may be responsible for its flexible structural behavior. PMID: 25483894
2. Data indicate that the RfaH transcriptional regulator protein beta-barrel conformation is much more stable than the alpha-helix conformation. PMID: 26033324
3. The importance of interfacial interactions between the two domains of RfaH is highlighted by the compromised structural integrity of the helical form of the C-terminal doamin in the absence N-terminal domain. PMID: 24758259
4. These results demonstrate a complex role for RfaH as a regulator of fimB expression via the suppression micA non-coding RNA. PMID: 24163336
5. The results indicate that all information necessary to control the folding of RfaH is encoded within RfaH itself, whereas accessory factors or sequential folding of N-terminal domain and C-terminal domain during translation are not essential for folding of active RfaH. PMID: 23990324
6. RfaH ai a transformer protein that uses two alternative folds to carry out two separate functions: autoinhibition of RNAP binding and recruitment of a ribosome. PMID: 23131843
7. Study shows that the released RfaH-carboxy-terminal domain (CTD) completely refolds from an all-alpha to an all-beta conformation identical to that of NusG-CTD. As a consequence, RfaH-CTD binding to S10 is enabled and translation of RfaH-controlled operons is strongly potentiated. PMID: 22817892
8. One side of RfaH(N) interacts with the non-template DNA strand during recruitment, whereas a hydrophobic surface on the opposite side of RfaH(N) remains bound to the beta' subunit clamp helices domain throughout transcription of the entire operon. PMID: 20132437
9. the regulatory effect of RfaH on LPS-core synthesis affects intestinal colonization PMID: 15727837
10. negatively controls expression and surface presentation of Ag43 and possibly another Ag43-independent factor(s) that mediates cell-cell interactions and biofilm formation. PMID: 16452414
11. we argue that RfaH binds to the beta' subunit coiled coil, the major target site for the initiation sigma factors. PMID: 17434131

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KEGG: ecj:JW3818

STRING: 316385.ECDH10B_4031