Perryman R A, Mooney B, Harmey M A
Department of Botany, University College Dublin, Belfield, Ireland.
Arch Biochem Biophys. 1995 Feb 1;316(2):659-64. doi: 10.1006/abbi.1995.1088.
A 42-kDa plant outer mitochondrial membrane protein, MOM42, has been identified as an essential component of the plant mitochondrial precursor protein translocation apparatus. Immunological cross-reactivity has been detected between antibodies raised against both Neurospora and yeast mitochondrial outer membrane proteins and plant mitochondrial outer membrane proteins. Immunocompetition studies showed that import of precursors to Rieske FeS protein, ATPase su9-DHFR, and the adenine nucleotide transporter was inhibited in the presence of antibody to MOM42. The inhibition of Rieske Fes and su9-DHFR import was greater than that of the adenine nucleotide transporter. The competition studies suggest that the MOM42 is involved in the translocation of bound precursor proteins. The import data and the Western blots suggest that components of the mitochondrial import system are highly conserved.
一种42千道尔顿的植物线粒体外膜蛋白MOM42,已被鉴定为植物线粒体前体蛋白转运装置的一个重要组成部分。针对粗糙脉孢菌和酵母线粒体外膜蛋白产生的抗体与植物线粒体外膜蛋白之间已检测到免疫交叉反应。免疫竞争研究表明,在存在抗MOM42抗体的情况下,Rieske FeS蛋白、ATPase su9-DHFR和腺嘌呤核苷酸转运体的前体导入受到抑制。Rieske Fes和su9-DHFR导入的抑制作用大于腺嘌呤核苷酸转运体。竞争研究表明,MOM42参与结合的前体蛋白的转运。导入数据和蛋白质免疫印迹表明,线粒体导入系统的组分高度保守。