The GT to GC single nucleotide polymorphism at the beginning of an alternative exon 2C of human MTH1 gene confers an amino terminal extension that functions as a mitochondrial targeting signal.

doi:10.1007/s00109-006-0053-5

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Article

The GT to GC single nucleotide polymorphism at the beginning of an alternative exon 2C of human MTH1 gene confers an amino terminal extension that functions as a mitochondrial targeting signal.

Journal of molecular medicine (Berlin, Germany) - 1 Aug 2006

Sakai Yasunari, Oda Hisanobu, Yoshimura Daisuke, Furuichi Masato, Kang Dongchon, Iwai Shigenori, Hara Toshiro, Nakabeppu Yusaku

Abstract excerpt

Human MTH1 protein hydrolyzes oxidized purine nucleotides 8-oxo-2'-deoxyguanosine triphosphate (8-oxo-dGTP), 2-OH-dATP or their ribo-forms to their monophosphates, thus minimizing replicational and transcriptional errors both in the nuclei and mitochondria. MTH1 suppresses mitochondrial dysfunction and cell death caused by H(2)O(2). Furthermore, MTH1 suppresses the transient increase in 8-oxoguanine in...

Topics

Adenosine Triphosphate
Alternative Splicing
Amino Acid Motifs
Amino Acid Sequence
Cell Line
DNA Repair Enzymes
Exons
Humans
Hydrolysis
Isoenzymes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mitochondria

Molecular Sequence Data

Phosphoric Monoester Hydrolases

Polymorphism, Single Nucleotide

Protein Sorting Signals

Protein Transport

Recombinant Fusion Proteins

Source

Open in PubMed

Identifiers

PMID: 16607562
DOI: 10.1007/s00109-006-0053-5

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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