CYTOLOGIA
Online ISSN : 1348-7019
Print ISSN : 0011-4545
New Protein Pmn34 with an Exonuclease Motif Localizes in the Mitochondrial Nucleoid Periphery of Physarum polycephalum
Kie ItohAkiko IzumiToshiyuki MoriNaoshi DohmaeRyoko YuiKatsura Maeda-SanoMasahiro M. KanaokaHaruko KuroiwaTsuneyoshi KuroiwaTetsuya HigashiyamaKimiko Murakami-MurofushiShigeyuki KawanoNarie Sasaki
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JOURNAL OPEN ACCESS

2009 Volume 74 Issue 4 Pages 401-407

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Abstract

Mitochondrial DNA (mtDNA) is highly organized into a compact structure, the mitochondrial nucleoid (mt-nucleoid). To facilitate our understanding of the regulation of mtDNA genetic activity within the mt-nucleoid structure, we have identified a novel mt-nucleoid protein Pmn34 (Physarum polycephalum mitochondrial nucleoid protein 34), having a molecular weight of 34 kDa, from pure mt-nucleoids isolated from the true slime mold, Physarum polycephalum. The Pmn34 protein is composed of 326 amino acids with mitochondrial transit peptides and its primary sequence contains a conserved 3′ to 5′ exonuclease motif of the “DEDD” superfamily. DNA mobility shift assays demonstrated that recombinant Pmn34 binds weakly to both mtDNA and λDNA with no apparent sequence specificity. Furthermore, immunoblotting and immunostaining analyses revealed that Pmn34 localizes specifically in the peripheral region of mt-nucleoids. These results indicate that Pmn34 functions in the peripheral region of mt-nucleoids, suggesting that the mt-nucleoid is compartmentalized into functional domains.

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© (2009), The Japan Mendel Society
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