Searle S, McCrossan M V, Smith D F
Department of Biochemistry, Imperial College of Science, Technology and Medicine, London, UK.
J Cell Sci. 1993 Apr;104 ( Pt 4):1091-100. doi: 10.1242/jcs.104.4.1091.
The DNA sequence has been determined of a gene from Leishmania major that shares sequence identity with members of the eukaryotic heat shock protein (hsp) 70 gene family. The deduced open reading frame for translation shares a number of features common to hsp70 stress proteins, including conserved amino acids implicated in ATP binding and a putative calmodulin-binding site. In addition, the protein has an N-terminal sequence characteristic of a mitochondrial targeting signal. Specific antibodies to this protein, generated by the use of recombinant fusion peptides, recognise a 65 kDa molecule of pI 6.7. This molecule is constitutively expressed and localises to the mitochondrion in all stages of the parasite life cycle. These features suggest a role for this protein as a molecular chaperone in Leishmania.
已确定来自硕大利什曼原虫的一个基因的DNA序列，该基因与真核热休克蛋白（hsp）70基因家族成员具有序列同一性。推导的用于翻译的开放阅读框具有hsp70应激蛋白共有的许多特征，包括与ATP结合有关的保守氨基酸和一个假定的钙调蛋白结合位点。此外，该蛋白质具有线粒体靶向信号的N端序列特征。通过使用重组融合肽产生的针对该蛋白质的特异性抗体识别出一个pI为6.7的65 kDa分子。该分子组成性表达，并在寄生虫生命周期的所有阶段定位于线粒体。这些特征表明该蛋白质在利什曼原虫中作为分子伴侣发挥作用。
