Aim23p Interacts with the Yeast Mitochondrial Ribosomal Small Subunit

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I. V. Chicherin¹, V. V. Zinina¹, S. A. Levitskiy¹, M. V. Serebryakova², and P. A. Kamenski^1,a*

¹Lomonosov Moscow State University, Faculty of Biology, 119991 Moscow, Russia

²Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia

^* To whom correspondence should be addressed.

Received August 23, 2018; Revised September 12, 2018; Accepted September 12, 2018

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Protein synthesis in mitochondria is generally organized in a bacterial-like manner but, at the same time, possesses several unique traits. Translation initiation in mitochondria is regulated by two protein factors, mtIF2 and mtIF3. Previously we demonstrated that Saccharomyces cerevisiae Aim23 protein is an ortholog of IF3 in budding yeast. However, the data on the interactions between Aim23p and other proteins are limited. Here, we demonstrated that Aim23p interacts with the yeast mitochondrial ribosomal small subunit both in vivo and in vitro using co-immunoprecipitation and density gradient sedimentation.

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KEY WORDS: mitochondria, translation, ribosomes, initiation factor, Aim23p

DOI: 10.1134/S000629791901005X

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