Upstream sequence of the parahydroxyphenyl-pyruvate dioxygenase (melA) coding region leading to enhanced expression in Shewanella colwelliana.
Hyperexpression of the enzyme, parahydroxyphenylpyruvate dioxygenase (pHPPH; melA), in the tyrosine degradative pathway yields excess homogentisic acid which oxidatively polymerizes to pyomelanin. Depression of melA in Shewanella colwelliana strain D was found to result from a single base pair transition upstream of the promoter. This was the sole lesion detected in pHPPH hyperexpressing strains. It is suggested that a T to C transition alters the mRNA structure, exposing the ribosome binding site, thereby enhancing translational efficiency.
Eylem
C L
CL
Department of Microbiology, University of Maryland, College Park 20742, USA.
Quintero
E J
EJ
Weiner
R M
RM
D015111:4-Hydroxyphenylpyruvate Dioxygenase / Q000235:genetics* / Q000378:metabolism; D001483:Base Sequence; D004269:DNA, Bacterial; D006092:Gram-Negative Facultatively Anaerobic Rods / Q000201:enzymology*; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011401:Promoter Regions, Genetic; D012329:RNA, Bacterial
D004269:DNA, Bacterial; D012329:RNA, Bacterial; D015111:4-Hydroxyphenylpyruvate Dioxygenase