Artículos de revistas
Characterization of a novel peroxisome membrane protein essential for conversion of isopenicillin N into cephalosporin C
Fecha
2010Registro en:
Biochemical Journal, Volumen 432, Issue 2, 2018, Pages 227-236
02646021
14708728
10.1042/BJ20100827
Autor
Ullán, Ricardo V.
Teijeira, Fernando
Guerra, Susana M.
Vaca Cerezo, Inmaculada
Martín, Juan F.
Institución
Resumen
The mechanisms of compartmentalization of intermediates and secretion of penicillins and cephalosporins in β-lactam antibiotic-producing fungi are of great interest. In Acremonium chrysogenum, there is a compartmentalization of the central steps of the CPC (cephalosporin C) biosynthetic pathway. In the present study, we found in the 'early' CPC cluster a new gene named cefP encoding a putative transmembrane protein containing 11 transmembrane spanner. Targeted inactivation of cefP by gene replacement showed that it is essential for CPC biosynthesis. The disrupted mutant is unable to synthesize cephalosporins and secretes a significant amount of IPN (isopenicillin N), indicating that the mutant is blocked in the conversion of IPN into PenN (penicillin N). The production of cephalosporin in the disrupted mutant was restored by transformation with both cefP and cefR (a regulatory gene located upstream of cefP), but not with cefP alone. Fluorescence microscopy studies with an EGFP (enhance