Expression and differential intracellular localization of two major forms of human 8-oxoguanine DNA glycosylase encoded by alternatively spliced OGG1 mRNAs
K Nishioka, T Ohtsubo, H Oda, T Fujiwara… - Molecular biology of …, 1999 - Am Soc Cell Biol
K Nishioka, T Ohtsubo, H Oda, T Fujiwara, D Kang, K Sugimachi, Y Nakabeppu
Molecular biology of the cell, 1999•Am Soc Cell BiolWe identified seven alternatively spliced forms of human 8-oxoguanine DNA glycosylase
(OGG1) mRNAs, classified into two types based on their last exons (type 1 with exon 7: 1a
and 1b; type 2 with exon 8: 2a to 2e). Types 1a and 2a mRNAs are major in human tissues.
Seven mRNAs are expected to encode different polypeptides (OGG1–1a to 2e) that share
their N terminus with the common mitochondrial targeting signal, and each possesses a
unique C terminus. A 36-kDa polypeptide, corresponding to OGG1–1a recognized only by …
(OGG1) mRNAs, classified into two types based on their last exons (type 1 with exon 7: 1a
and 1b; type 2 with exon 8: 2a to 2e). Types 1a and 2a mRNAs are major in human tissues.
Seven mRNAs are expected to encode different polypeptides (OGG1–1a to 2e) that share
their N terminus with the common mitochondrial targeting signal, and each possesses a
unique C terminus. A 36-kDa polypeptide, corresponding to OGG1–1a recognized only by …
We identified seven alternatively spliced forms of human 8-oxoguanine DNA glycosylase (OGG1) mRNAs, classified into two types based on their last exons (type 1 with exon 7: 1a and 1b; type 2 with exon 8: 2a to 2e). Types 1a and 2a mRNAs are major in human tissues. Seven mRNAs are expected to encode different polypeptides (OGG1–1a to 2e) that share their N terminus with the common mitochondrial targeting signal, and each possesses a unique C terminus. A 36-kDa polypeptide, corresponding to OGG1–1a recognized only by antibodies against the region containing helix-hairpin-helix-PVD motif, was copurified from the nuclear extract with an activity introducing a nick into DNA containing 8-oxoguanine. A 40-kDa polypeptide corresponding to a processed form of OGG1–2a was detected in their mitochondria using antibodies against its C terminus. Electron microscopic immunocytochemistry and subfractionation of the mitochondria revealed that OGG1–2a locates on the inner membrane of mitochondria. Deletion mutant analyses revealed that the unique C terminus of OGG1–2a and its mitochondrial targeting signal are essential for mitochondrial localization and that nuclear localization of OGG1–1a depends on the NLS at its C terminus.
Am Soc Cell Biol
