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. 2015:2015:452958.
doi: 10.1155/2015/452958. Epub 2015 May 31.

Comparative Analysis of Apicoplast-Targeted Protein Extension Lengths in Apicomplexan Parasites

Alexandr V Seliverstov  1 , Oleg A Zverkov  1 , Svetlana N Istomina  1 , Sergey A Pirogov  1 , Philip S Kitsis  1
Affiliations

Comparative Analysis of Apicoplast-Targeted Protein Extension Lengths in Apicomplexan Parasites

Alexandr V Seliverstov et al. Biomed Res Int. 2015.

Abstract

In general, the mechanism of protein translocation through the apicoplast membrane requires a specific extension of a functionally important region of the apicoplast-targeted proteins. The corresponding signal peptides were detected in many apicomplexans but not in the majority of apicoplast-targeted proteins in Toxoplasma gondii. In T. gondii signal peptides are either much diverged or their extension region is processed, which in either case makes the situation different from other studied apicomplexans. We propose a statistic method to compare extensions of the functionally important regions of apicoplast-targeted proteins. More specifically, we provide a comparison of extension lengths of orthologous apicoplast-targeted proteins in apicomplexan parasites. We focus on results obtained for the model species T. gondii, Neospora caninum, and Plasmodium falciparum. With our method, cross species comparisons demonstrate that, in average, apicoplast-targeted protein extensions in T. gondii are 1.5-fold longer than in N. caninum and 2-fold longer than in P. falciparum. Extensions in P. falciparum less than 87 residues in size are longer than the corresponding extensions in N. caninum and, reversely, are shorter if they exceed 88 residues.

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Figures

Figure 1
Figure 1
Plot of protein length extensions in T. gondii ME49 versus N. caninum relative to their orthologs in Synechocystis sp. PCC 6803. Differences in lengths between sporozoan and cyanobacterial orthologous proteins are plotted as follows: T-S on the x-axis, N-S on the y-axis.
Figure 2
Figure 2
Plot of protein length extensions in T. gondii ME49 versus P. falciparum 3D7 relative to their orthologs in Synechocystis sp. PCC 6803. Differences in lengths between sporozoan and cyanobacterial orthologous proteins are plotted as follows: T-S on the x-axis, P-S on the y-axis.
Figure 3
Figure 3
Plot of protein length extensions in N. caninum Liverpool versus P. falciparum 3D7 relative to their orthologs in Synechocystis sp. PCC 6803. Differences in lengths between sporozoan and cyanobacterial orthologous proteins are plotted as follows: N-S on the x-axis, P-S on the y-axis.
Figure 4
Figure 4
Some apicoplast-targeted proteins in T. gondii containing serine-rich regions. The region coordinates indicated on the left and the protein lengths on the right. The serine-rich regions are arranged irregularly, which is confirmed on a larger number of proteins for different pairs, triples, and so forth of amino acids.
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