Protein import complexes in the mitochondrial outer membrane of Amoebozoa representatives. (December 2016)

• Record Type: Journal Article
• Authors: Buczek, Dorota; Wojtkowska, Małgorzata; Suzuki, Yutaka; Sonobe, Seiji; Nishigami, Yukinori; Antoniewicz, Monika; Kmita, Hanna; Makałowski, Wojciech
• Is Part Of: BMC genomics. Volume 17:Number 1(2016)
• Page Start: 1
• Page End: 16
• Publication Date: 2016-12
• Subjects: Amoebozoa -- Protein import into mitochondria -- Transcriptome analysis -- TOM complex -- TOB/SAM complex -- ERMES complex; Genomes -- Periodicals; Gene mapping -- Periodicals; Genomics -- Periodicals; Base Sequence -- Periodicals; Chromosome Mapping -- Periodicals; Genetic Techniques -- Periodicals; Sequence Analysis, DNA -- Periodicals; 572.8605
• DOI: 10.1186/s12864-016-2402-2
• Languages: English
• ISSNs: 1471-2164

Abstract

Abstract Background An ancestral trait of eukaryotic cells is the presence of mitochondria as an essential element for function and survival. Proper functioning of mitochondria depends on the import of nearly all proteins that is performed by complexes located in both mitochondrial membranes. The complexes have been proposed to contain subunits formed by proteins common to all eukaryotes and additional subunits regarded as lineage specific. Since Amoebozoa is poorly sampled for the complexes we investigated the outer membrane complexes, namely TOM, TOB/SAM and ERMES complexes, using available genome and transcriptome sequences, including transcriptomes assembled by us. Results The results indicate differences in the organization of the Amoebozoa TOM, TOB/SAM and ERMES complexes, with the TOM complex appearing to be the most diverse. This is reflected by differences in the number of involved subunits and in similarities to the cognate proteins of representatives from different supergroups of eukaryotes. Conclusions The obtained results clearly demonstrate structural variability/diversity of these complexes in the Amoebozoa lineage and the reduction of their complexity as compared with the same complexes of model organisms.