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Publication : Expression analysis and mitochondrial targeting properties of the chicken manganese-containing superoxide dismutase.

First Author  Kong BW Year  2003
Journal  Biochim Biophys Acta Volume  1625
Issue  1 Pages  98-108
PubMed ID  12527430 Mgi Jnum  J:81199
Mgi Id  MGI:2448231 Doi  10.1016/s0167-4781(02)00593-6
Citation  Kong BW, et al. (2003) Expression analysis and mitochondrial targeting properties of the chicken manganese-containing superoxide dismutase. Biochim Biophys Acta 1625(1):98-108
abstractText  Manganese-containing superoxide dismutase (MnSOD) is a major detoxifying enzyme that functions in cellular oxygen metabolism by converting O(2)(-) to H(2)O(2). A cDNA encoding the chicken MnSOD (cMnSOD) has been isolated from a chicken embryo fibroblast (CEF) cell cDNA library. The cloned cMnSOD is 1102 bp in length with an open reading frame (ORF) of 224 amino acids that includes a 26-amino-acid 5'-proximal mitochondrial targeting sequence (MTS). The mature 198-amino-acid region of the cMnSOD is highly conserved among various mammalian species. Two cMnSOD mRNA species (1.2 and 1.0 kb) were expressed in most of the tissues and organs analyzed, with the highest expression levels found in brain, kidney, and heart tissues. Compared to earlier stages of development, expression of cMnSOD was highest in day 13 embryonic heart tissue, and was maintained until post-hatch. Exogenously introduced cMnSOD-GFP fusion constructs (which included the MTS) clearly accumulated in the mitochondria of chicken cells, as expected. Surprisingly, the cMnSOD MTS signal, which displays little similarity to mammalian MTS sequences, enabled cMnSOD-GFP fusion proteins to target mitochondria not only from different cell types (fibroblastic and epithelial), but from a number of mammalian species (human, mouse, and pig). This suggests that specific amino acid motifs within the MTS domain may be more important than the overall sequence similarities for mitochondrial targeting.
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