Turkarslan Serdar, Sanders Carsten, Daldal Fevzi
University of Pennsylvania, Department of Biology, Plant Science Institute, Philadelphia, PA 19104, USA.
Mol Microbiol. 2006 May;60(3):537-41. doi: 10.1111/j.1365-2958.2006.05148.x.
In all organisms, haem is post-translationally and covalently attached to c apocytochromes to produce c holocytochromes via a process called c-type cytochromes maturation, which involves numerous components. In bacteria it was not clear which of these components catalyses the extracytoplasmic haem-apocytochrome ligation per se. In this issue of Molecular Microbiology, Feissner and colleagues report that a single polypeptide from Helicobacter pylori, corresponding to the fusion of two proteins found in other organisms, performs haem ligation to a coexpressed Bordetella pertussis apocytochrome c in an Escherichia coli mutant lacking its own cytochrome c maturation proteins. This simple experimental system pinpoints the components catalysing extracytoplasmic covalent haem ligation and raises intriguing issues about the requirements for delivery of haem and apocytochrome c substrates to produce c holocytochromes.
在所有生物体中,血红素通过一种称为c型细胞色素成熟的过程在翻译后与脱辅基细胞色素共价结合,以产生全细胞色素,这一过程涉及众多组分。在细菌中,尚不清楚这些组分中哪一个本身催化胞外血红素-脱辅基细胞色素连接。在本期《分子微生物学》中,费斯纳及其同事报告称,幽门螺杆菌中的一种单一多肽,相当于在其他生物体中发现的两种蛋白质的融合体,在缺乏自身细胞色素c成熟蛋白的大肠杆菌突变体中,将血红素连接到共表达的百日咳博德特氏菌脱辅基细胞色素c上。这个简单的实验系统确定了催化胞外共价血红素连接的组分,并引发了关于将血红素和脱辅基细胞色素c底物递送至产生全细胞色素的要求的有趣问题。