A Small Tim Homohexamer in the Relict Mitochondrion of Cryptosporidium

被引:15
作者
Alcock, Felicity [1 ]
Webb, Chaille T. [1 ]
Dolezal, Pavel [2 ]
Hewitt, Victoria [1 ]
Shingu-Vasquez, Miguel [1 ]
Likic, Vladimir A. [3 ]
Traven, Ana [1 ]
Lithgow, Trevor [1 ]
机构
[1] Monash Univ, Dept Biochem & Mol Biol, Clayton, Vic, Australia
[2] Charles Univ Prague, Dept Parasitol, Prague 2, Czech Republic
[3] Univ Melbourne, Mol Sci & Biotechnol Inst Bio21, Parkville, Vic 3052, Australia
基金
澳大利亚研究理事会; 英国医学研究理事会;
关键词
mitochondria; mitosomes; protein import; protein evolution; molecular machines; PROTEIN IMPORT CHANNEL; INTERMEMBRANE SPACE; OUTER-MEMBRANE; METABOLIC PATHWAYS; COMPLEX; EVOLUTION; BIOGENESIS; MIA40; APICOMPLEXAN; RESIDUES;
D O I
10.1093/molbev/msr165
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The apicomplexan parasite Cryptosporidium parvum possesses a mitosome, a relict mitochondrion with a greatly reduced metabolic capability. This mitosome houses a mitochondrial-type protein import apparatus, but elements of the protein import pathway have been reduced, and even lost, through evolution. The small Tim protein family is a case in point. The genomes of C. parvum and related species of Cryptosporidium each encode just one small Tim protein, CpTimS. This observation challenged the tenet that small Tim proteins are always found in pairs as alpha(3)beta(3) hexamers. We show that the atypical CpTimS exists as a relatively unstable homohexamer, shedding light both on the early evolution of the small Tim protein family and on small Tim hexamer formation in contemporary eukaryotes.
引用
收藏
页码:113 / 122
页数:10
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