Biochemical properties of Caenorhabditis elegans HMG-5, a regulator of mitochondrial DNA.

Abstract:

:Caenorhabditis elegans HMG-5, which is encoded by F45E4.9, contains two high mobility group (HMG) box domains and shows sequence similarity with mammalian mitochondrial transcription factor A (TFAM). In this study, using soaking RNA interference, we found that knockdown of HMG-5 reduced the amount of mtDNA in P0 hermaphrodites, suggesting it as functional orthologue of mammalian TFAM. We also examined the biochemical property of HMG-5 in mammalian cells and in vitro. We found that HMG-5 localized to the mitochondria in human cultured cells and was included in the NP-40-insoluble fraction in which mtDNA and TFAM were enriched. By immunoprecipitation analysis, HMG-5 was found to associate with human mitochondrial DNA (mtDNA) in the cells. In vitro binding experiment also showed that HMG-5 binds to C. elegans mtDNA and plasmid DNA, indicating its feature as a non-specific DNA-binding protein. Furthermore, it was found that HMG-5 can interact with itself. These results demonstrate that HMG5 shares similar biochemical properties with mammalian TFAM as a nucleoid factor. HMG-5 could be a good candidate for investigating mtDNA metabolism in multicellular organisms.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Sumitani M,Kasashima K,Matsugi J,Endo H

doi

10.1093/jb/mvr008

subject

Has Abstract

pub_date

2011-05-01 00:00:00

pages

581-9

issue

5

eissn

0021-924X

issn

1756-2651

pii

mvr008

journal_volume

149

pub_type

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