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Tyrosine phosphorylation of BipA and its effect on the binding affinity of BipA
Author(s) -
Blaha Gregor,
Conn Adam,
Fan Haitian,
Hahm Joseph,
Diggs Stephen,
Preston Williams,
Wang Yinsheng
Publication year - 2016
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.30.1_supplement.1066.1
Subject(s) - gtpase , phosphorylation , microbiology and biotechnology , tyrosine , tyrosine phosphorylation , biochemistry , ribosome , intracellular , biology , chemistry , rna , gene
BipA is a translational GTPase with homology to translational elongation factor‐G. BipA changes its binding preference from ribosome to small ribosomal subunit depending on the intracellular ppGpp concentration. The cellular levels of ppGpp are correlated inversely to the availability of nutrients. BipA is also known to be responsible for interactions between enteropathogenic E. coli (EPEC) and human small‐intestinal epithelial cells in vitro . BipA knock out mutants of EPEC cannot attach and efface intestinal cells. BipA is tyrosine‐phosphorylated in vivo but only in the pathogenic strains of E. coli such as EPEC. We identified the specific residues that are in vitro phosphorylated and determined their effect on the BipA's binding affinity for ppGpp, ribosomes, and ribosomal subunits.