Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9573591 | Biophysical Chemistry | 2005 | 4 Pages |
Abstract
Translation in all open reading frames (ORF) of human ceruloplasmin (Cp) pseudogene revealed the only translating sequence of 984 nucleotides. The amino acid sequence contains a signal peptide for mitochondrial protein import at N-terminus. The predicted protein without taking the signal peptide into consideration has 92% identity to the corresponding Cp fragment. It contains 20 amino acid substitutions, 8 of them are significant. There is His-X-His motif in the center of a molecule that is typical for copper containing oxidases. Potential copper-binding site appears as a result of the substitution P923H along human Cp sequence. Cp pseudogene transcription product was found in the cultured human cell lines HepG2 and HuTu 80 using RT-PCR strategy. Cp polypeptides with molecular weight of nearly 30 kDa were found in mitochondria of HuTu 80 cells. The possible biological role of mitochondrial Cp is under discussion.
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Chemistry
Physical and Theoretical Chemistry
Authors
N.A. Platonova, A.V. Vasin, S.A. Klotchenko, N.V. Tsymbalenko, L.V. Puchkova,