![]() ![]() To determine the in vivo consequences of phosphorylation, infection experiments were performed in bone marrow-derived macrophages and in mice using threonine-to-alanine mutants of Rv1747 that prevent specific phosphorylation and revealed that phosphorylation positively modulates Rv1747 function in vivo. Experiments to determine how PknF regulates the function of Rv1747 demonstrated that phosphorylation occurs on two specific threonine residues, Thr-150 and Thr-208. FHA domains are phosphopeptide recognition motifs that specifically recognize phosphothreonine-containing epitopes. tuberculosis in vivo and contains two forkhead-associated (FHA) domains. This study concerns one of these enzymes, the serine/threonine protein kinase PknF, that is encoded in an operon with Rv1747, an ABC transporter that is necessary for growth of M. One major signaling method employed by Mycobacterium tuberculosis, the causative agent of tuberculosis, is through reversible phosphorylation of proteins mediated by protein kinases and phosphatases. Rodgers, Angela Leiba, Jade Stach, Lasse Walker, K. Generally, written and telegraphy examinations for.įorkhead-associated (FHA) Domain Containing ABC Transporter Rv1747 Is Positively Regulated by Ser/Thr Phosphorylation in Mycobacterium tuberculosis* 0.485 Section 0.485 Telecommunication FEDERAL COMMUNICATIONS COMMISSION GENERAL COMMISSION ORGANIZATION General.485 Commercial radio operator examinations. ![]() 47 Telecommunication 1 false Commercial radio operator examinations. The divergent aberrant PIM profiles and the opposing in vivo growth phenotypes of Δ Rv2623 and Δ Rv1747, together with the annotated lipooligosaccharide exporter function of Rv1747, suggest that Rv2623 interacts with Rv1747 to modulate mycobacterial growth by negatively regulating the activity of Rv1747 and that RvĤ7 CFR 0.485 - Commercial radio operator examinations. Collectively, these data have provided evidence that Rv2623 interacts with Rv1747 to regulate mycobacterial growth and this interaction is mediated via the recognition of the conserved Rv2623 pT237-containing FHA-binding motif by the Rv1747 FHA I domain. ![]() Animal studies have previously shown that Δ Rv2623 is hypervirulent, while Δ Rv1747 is growth-attenuated. tuberculosis Rv2623 null mutant (Δ Rv2623) displays enhanced expression of phosphatidyl-myo-inositol mannosides (PIMs), while the Δ Rv1747 mutant expresses decreased levels of PIMs. Interestingly, compared to WT bacilli, an M. Relative to wild-type Rv2623 ( Rv2623WT), a mutant protein in which T237 has been replaced with a non-phosphorylatable alanine ( Rv2623T237A) exhibits decreased interaction with the Rv1747 FHA I domain and diminished growth-regulatory capacity. Biochemical, immunochemical and mass spectrometric studies have shown that Rv2623 harbors pT and specifically identified threonine 237 as a phosphorylated residue. FHA domains are signaling protein modules that mediate protein-protein interactions to modulate a wide variety of biological processes via binding to conserved phosphorylated threonine (pT)-containing oligopeptides of the interactors. Here, yeast two-hybrid and affinity chromatography experiments have demonstrated that Rv2623 interacts with one of the two forkhead-associated domains (FHA I) of Rv1747, a putative ATP-binding cassette transporter annotated to export lipooligosaccharides. ![]() We have previously shown that the Mycobacterium tuberculosis universal stress protein Rv2623 regulates mycobacterial growth and may be required for the establishment of tuberculous persistence. Glass, Lisa N Swapna, Ganduri Chavadi, Sivagami Sundaram Tufariello, JoAnn M Mi, Kaixia Drumm, Joshua E Lam, TuKiet T Zhu, Guofeng Zhan, Chenyang Vilchéze, Catherine Arcos, Jesus Chen, Yong Bi, Lijun Mehta, Simren Porcelli, Steven A Almo, Steve C Yeh, Syun-Ru Jacobs, William R Torrelles, Jordi B Chan, John Mycobacterium tuberculosis universal stress protein Rv2623 interacts with the putative ATP binding cassette (ABC) transporter Rv1747 to regulate mycobacterial growth. ![]()
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