Bisson R, Vettore S, Aratri E, Sandona D
Centro CNR Biomembrane and Dipartimento di Scienze Biomediche Sperimentali, Padova, Italy.
EMBO J. 1997 Feb 17;16(4):739-49. doi: 10.1093/emboj/16.4.739.
Cytochrome c oxidase (COX) has a complex modular structure in eukaryotes. Depending on growth conditions, interchangeable isoforms of selected subunits are synthesized and combined to the evolutionarily conserved catalytic core of the enzyme. In Dictyostelium this structural make-up is regulated by oxygen and involves two forms of the smallest subunit, termed VIIe and VIIs. Here we show that, in spite of a considerable sequence divergency, they are encoded by adjacent genes, linked 'tail to head' by only 800 bp. Deletion analyses reveal the presence of a short intergenic segment acting as an oxygen transcriptional switch. This structural organization and the different stability of the two subunit isoforms offer a molecular explanation for the extraordinary sensitivity to oxygen of the switching mechanism.
细胞色素c氧化酶(COX)在真核生物中具有复杂的模块化结构。根据生长条件,会合成选定亚基的可互换同工型,并将其组合到该酶进化上保守的催化核心中。在盘基网柄菌中,这种结构组成受氧气调节,涉及最小亚基的两种形式,称为VIIe和VIIs。在这里,我们表明,尽管序列差异很大,但它们由相邻基因编码,仅通过800 bp“头对头”相连。缺失分析揭示了存在一个短的基因间隔区段,其作为氧气转录开关。这种结构组织以及两种亚基同工型的不同稳定性为转换机制对氧气的非凡敏感性提供了分子解释。