Merriman T R, Merriman M E, Lamont I L
Department of Biochemistry, University of Otago, Dunedin, New Zealand.
J Bacteriol. 1995 Jan;177(1):252-8. doi: 10.1128/jb.177.1.252-258.1995.
Pseudomonas aeruginosa secretes a fluorescent siderophore, pyoverdine, when grown under iron-deficient conditions. Pyoverdine consists of a chromophoric group bound to a partly cyclic octapeptide. As a step toward understanding the molecular events involved in pyoverdine synthesis, we have sequenced a gene, pvdD, required for this process. The gene encodes a 2,448-residue protein, PvdD, which has a predicted molecular mass of 273,061 Da and contains two highly similar domains of about 1,000 amino acids each. The protein is similar to peptide synthetases from a range of bacterial and fungal species, indicating that synthesis of the peptide moiety of pyoverdine proceeds by a nonribosomal mechanism. The pvdD gene is adjacent to a gene, fpvA, which encodes an outer membrane receptor protein required for uptake of ferripyoverdine.
铜绿假单胞菌在缺铁条件下生长时会分泌一种荧光铁载体——绿脓菌素。绿脓菌素由一个与部分环状八肽结合的发色基团组成。作为理解绿脓菌素合成所涉及分子事件的第一步，我们对该过程所需的一个基因pvdD进行了测序。该基因编码一种由2448个氨基酸残基组成的蛋白质PvdD，预测分子量为273061道尔顿，且包含两个高度相似的结构域，每个结构域约有1000个氨基酸。该蛋白质与一系列细菌和真菌物种的肽合成酶相似，这表明绿脓菌素肽部分的合成是通过非核糖体机制进行的。pvdD基因与一个基因fpvA相邻，fpvA编码一种摄取铁绿脓菌素所需的外膜受体蛋白。
