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BrgE is a regulator of Myxococcus xanthus development
Author(s) -
Pham Vinh D.,
Shebelut Conrad W.,
Zumstein Erin J.,
Singer Mitchell
Publication year - 2005
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2005.04726.x
Subject(s) - myxococcus xanthus , biology , mutant , response regulator , signal transduction , regulator , wild type , phenotype , mutation , yeast , genetics , amino acid , microbiology and biotechnology , biochemistry , gene
Summary We report here the identification and characterization of a member of the Myxococcus xanthus SdeK signal transduction pathway, BrgE. This protein was identified as an SdeK‐interacting component using a yeast two‐hybrid screen, and we further confirmed this interaction by the glutathione S‐transferase (GST) pulldown assay. Additional yeast two‐hybrid analyses revealed that BrgE preferentially interacts with the putative amino‐terminal sensor domain of SdeK, but not with the carboxy‐terminal kinase domain. A brgE insertion strain was shown to be blocked in development between aggregation and mound formation, and decreased by 50‐fold in viable spore production compared with the parental wild type. These phenotypes are similar to those of sdeK mutants. The brgE mutation also altered expression of a sample of Tn 5 lac developmental markers that are also SdeK regulated. Finally, we demonstrated that a brgE sdeK double mutant has a more severe sporulation defect than either of the two single mutants, suggesting that BrgE and SdeK act synergistically to regulate wild‐type levels of sporulation. In sum, these data suggest that BrgE operates as an auxiliary factor to stimulate the SdeK signal transduction pathway by directly binding to the amino‐terminal sensor domain of SdeK.