New Protein Pmn34 with an Exonuclease Motif Localizes in the Mitochondrial Nucleoid Periphery of Physarum polycephalum

Autor: Masahiro M. Kanaoka, Haruko Kuroiwa, Akiko Izumi, Tetsuya Higashiyama, Narie Sasaki, Tsuneyoshi Kuroiwa, Shigeyuki Kawano, Kimiko Murakami-Murofushi, Katsura Maeda-Sano, Naoshi Dohmae, Ryoko Yui, Toshiyuki Mori, Kie Itoh
Rok vydání: 2009
Předmět:
Zdroj: CYTOLOGIA. 74:401-407
ISSN: 1348-7019
0011-4545
Popis: 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.
Databáze: OpenAIRE