Literature DB >> 21910249

A third of the yeast mitochondrial proteome is dual localized: a question of evolution.

Reut Ben-Menachem1, Merav Tal, Tanya Shadur, Ophry Pines.   

Abstract

There are a growing number of examples of identical or almost identical proteins, which are localized to two (or more) separate compartments, a phenomenon that is termed protein dual localization, dual distribution or dual targeting. We previously divided a reference set of known yeast mitochondrial proteins into two groups, suggested to be dual localized or exclusive mitochondrial proteins. Here we examined this evaluation by screening 320 mitochondrial gene products for dual targeting, using the α-complementation assay. The analysis of the results of this experimentally independent screen supports our previous evaluation that dual localized mitochondrial proteins constitute a subgroup of mitochondrial proteins with distinctive properties. These proteins are characterized by a lower probability of mitochondrial localization (MitoProtII score), a lower net charge and are enriched for proteins with a weaker mitochondrial targeting sequence. Conversely, mRNAs of exclusive mitochondrial proteins are enriched in polysomes associated with mitochondria. Based on the discovery of more than 60 new gene products that are now assumed to be dual targeted, we have updated an annotation list of dual-targeted proteins. We currently estimate that more than a third of the mitochondrial proteome is dual targeted, and suggest that this abundant dual targeting presents an evolutionary advantage.
Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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Year:  2011        PMID: 21910249     DOI: 10.1002/pmic.201100199

Source DB:  PubMed          Journal:  Proteomics        ISSN: 1615-9853            Impact factor:   3.984


  30 in total

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4.  Cysteine desulfurase is regulated by phosphorylation of Nfs1 in yeast mitochondria.

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5.  Spatial distribution of cellular function: the partitioning of proteins between mitochondria and the nucleus in MCF7 breast cancer cells.

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8.  Linkage of oxidative stress and mitochondrial dysfunctions to spontaneous culture degeneration in Aspergillus nidulans.

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10.  Multiple proteins with essential mitochondrial functions have glycosylated isoforms.

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Journal:  Mitochondrion       Date:  2012-05-04       Impact factor: 4.160

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