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A Small Tim Homohexamer in the Relict Mitochondrion of Cryptosporidium
Author(s) -
Felicity Alcock,
Chaille T. Webb,
Pavel Doležal,
Victoria L. Hewitt,
Miguel Shingu-Vasquez,
Vladimir A. Likić,
Ana Traven,
Trevor Lithgow
Publication year - 2011
Publication title -
molecular biology and evolution
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.637
H-Index - 218
eISSN - 1537-1719
pISSN - 0737-4038
DOI - 10.1093/molbev/msr165
Subject(s) - biology , cryptosporidium , cryptosporidium parvum , genome , mitochondrion , protein family , random hexamer , apicomplexa , genetics , mitochondrial dna , evolutionary biology , gene , microbiology and biotechnology , plasmodium falciparum , immunology , malaria , feces
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 α3β3 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.

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