Article Dans Une Revue Biochemical Journal Année : 2010

Characterization of a novel peroxisome membrane protein essential for conversion of isopenicillin N to cephalosporin C

Ricardo V. Ullán
  • Fonction : Auteur
Fernando Teijeira
  • Fonction : Auteur
Susana M. Guerra
  • Fonction : Auteur
Inmaculada Vaca
  • Fonction : Auteur
Juan F. Martín
  • Fonction : Auteur correspondant
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Résumé

The mechanisms of compartmentalization of intermediates and secretion of penicillins and cephalosporins in β-lactam producing fungi are of great interest. In Acremonium chrysogenum there is a compartmentalization of the central steps of the cephalosporin C biosynthetic pathway. In this work, we found in the ‘early' cephalosporin C cluster a new gene named cefP encoding a putative transmembrane protein containing eleven transmembrane spanners. Targeted inactivation of cefP by gene replacement showed that it is essential for cephalosporin C biosynthesis. The disrupted mutant is unable to synthesize cephalosporins and secretes a significant amount of isopenicillin N indicating that the mutant is blocked in the conversion of isopenicillin N to penicillin N. The production of cephalosporin in the disrupted mutant was restored by transformation with both the cefP and cefR genes (a regulatory gene located upstream of cefP gene) but not with the cefP gene alone. Fluorescent microscopy studies with an eGFP-SKL protein (peroxisomal-targeted marker) as control showed that the red fluorescent CefP protein colocalized in the peroxisomes with the control peroxisomal protein. In summary, CefP is a peroxisomal membrane protein probably involved in the import of isopenicillin N into the peroxisomes where it is converted to penicillin N by the two-component CefD1-CefD2 protein system.

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hal-00535584 , version 1 (12-11-2010)

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Ricardo V. Ullán, Fernando Teijeira, Susana M. Guerra, Inmaculada Vaca, Juan F. Martín. Characterization of a novel peroxisome membrane protein essential for conversion of isopenicillin N to cephalosporin C. Biochemical Journal, 2010, 432 (2), pp.227-236. ⟨10.1042/BJ20100827⟩. ⟨hal-00535584⟩

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