Summary
The cytosolic molecular chaperone Hsp70 discriminates between the cytosolic (cAAT) and mitochondrial (mAAT) aspartate aminotransferase isozymes, recognizing and binding exclusively mAAT. By screening a library of synthetic peptides, we have identified six putative Hsp70binding sites in mAAT. Phylogenetic analyses indicate that these Hsp70-binding sequences show less variability in mAAT than cAAT and contain more fixed differences between the two isozymes than the rest of the sequence. Thus, sequence variation between cAAT and mAAT might direct their selective interaction with molecular chaperones and thereby contribute to their correct localization in the cell.
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Artigues, A., Bengoechea-Alonso, M.T., Crawford, D.L., Iriarte, A., Martinez-Carrion, M. (2000). Biological Implications of the Different Hsp70 Binding Properties of Mitochondrial and Cytosolic Aspartate Aminotransferase.. In: Iriarte, A., Martinez-Carrion, M., Kagan, H.M. (eds) Biochemistry and Molecular Biology of Vitamin B6 and PQQ-dependent Proteins. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8397-9_18
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DOI: https://doi.org/10.1007/978-3-0348-8397-9_18
Publisher Name: Birkhäuser, Basel
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