Isolation of a pdxJ point mutation that bypasses the requirement for the PdxH oxidase in pyridoxal 5' -phosphate coenzyme biosynthesis in Escherichia coli K-12.
We isolated 26 suppressor mutations that allowed growth of a delta pdxH::omega null mutant in the absence of pyridoxal. Each suppressor mapped to pdxJ, and the eight suppressors sequenced contained the same glycine-to-serine change in the PdxJ polypeptide. This bypass suppression suggests that PdxJ may participate in formation of the pyridine ring of pyridoxine 5'-phosphate.
Man
T K
TK
Department of Microbiology and Molecular Genetics, University of Texas Houston Medical School 77030-1501, USA.
Zhao
G
G
Winkler
M E
ME
D001426:Bacterial Proteins / Q000235:genetics*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D029968:Escherichia coli Proteins; D008025:Ligases; D008954:Models, Biological; D016254:Mutagenesis, Insertional; D017354:Point Mutation; D011732:Pyridoxal Phosphate / Q000031:analogs & derivatives / Q000096:biosynthesis* / Q000378:metabolism; D011734:Pyridoxaminephosphate Oxidase / Q000235:genetics / Q000378:metabolism; D017384:Sequence Deletion; D013489:Suppression, Genetic
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C098854:PdxJ protein, E coli; D011732:Pyridoxal Phosphate; D011734:Pyridoxaminephosphate Oxidase; D008025:Ligases; C024593:pyridoxine 5-phosphate