NDLI: Shot-gun proteomic analysis of mitochondrial D-loop DNA binding proteins: identification of mitochondrial histones

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Molecular BioSystems Vol - 7 Issue - 4

Molecular BioSystems Vol - 7 Issue - 3

Molecular BioSystems Vol - 7 Issue - 2

Molecular BioSystems Vol -6

Molecular BioSystems Vol -5

Molecular BioSystems Vol -4

Molecular BioSystems Vol -3

Molecular BioSystems Vol -2

Shot-gun proteomic analysis of mitochondrial D-loop DNA binding proteins: identification of mitochondrial histones

Content Provider	Royal Society of Chemistry (RSC)
Author	Choi, Yon-Sik Jung, Hee-Jung Pak, Youngmi Kim Hwang, Daehee Lee, Sang-Won Jeong, Jae Hoon Min, Hye-Ki
Copyright Year	2011
Abstract	Transcription and replication of mitochondrial DNA (mtDNA) are regulated by nuclear DNA-encoded proteins that are targeted into mitochondria. A decrease in mtDNA copy number results in mitochondrial dysfunction, which may lead to insulin resistance and metabolic syndromes. We analyzed mitochondrial proteins that physically bind to human mitochondrial D-loop DNA using a shot-gun proteomics approach following protein enrichment by D-loop DNA-linked affinity chromatography. A total of 152 D-loop DNA binding proteins were identified by peptide sequencing using ultra high pressure capillary reverse-phase liquid chromatography/tandem mass spectrometry. Bioinformatic analysis showed that 68 were mitochondrial proteins, 96 were DNA/RNA/protein binding proteins and 114 proteins might form a complex viaprotein–protein interactions. Histone family members of H1, H2A, H2B, H3, and H4, were detected in abundance among them. In particular, histones H2A and H2B were present in the mitochondrial membrane as integral membrane proteins and not bound directly to mtDNA inside the organelle. Histones H1.2, H3 and H4 were associated with the outer mitochondrial membrane. Silencing of H2AX expression inhibited mitochondrial protein transport. Our data suggests that many mitochondrial proteins may reside in multiple subcellular compartments like H2AX and exert multiple functions.
Starting Page	1523
Ending Page	1536
Page Count	14
File Format	HTM / HTML PDF
ISSN	1742206X
Volume Number	7
Issue Number	5
Journal	Molecular BioSystems
DOI	10.1039/c0mb00277a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Histone H2B H2AFX Mitochondrial DNA Protein Mitochondrion Affinity chromatography DNA Proteomics Organelle Insulin resistance Integral D-loop Peptide Mass spectrometry
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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