The Spring 2012 season of CACAO has started!
PMID:8248235
From GONUTS
Wang, N, Gottesman, S, Willingham, MC, Gottesman, MM and Maurizi, MR (1993) A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease.Proc. Natl. Acad. Sci. U.S.A. 90:11247-51
| Abstract | We have cloned a human ATP-dependent protease that is highly homologous to members of the bacterial Lon protease family. The cloned gene encodes a protein of 963 amino acids with a calculated molecular mass of 106 kDa, slightly higher than that observed by Western blotting the protein from human tissues and cell lines (100 kDa). A single species of mRNA was found for this Lon protease in all human tissues examined. The protease is encoded in the nucleus, and the amino-terminal portion of the protein sequence contains a potential mitochondrial targeting presequence. Immunofluorescence microscopy suggested a predominantly mitochondrial localization for the Lon protease in cultured human cells. A truncated LON gene, in which translation was initiated at Met118 of the coding sequence, was expressed in Escherichia coli and produced a protease that degraded alpha-casein in vitro in an ATP-dependent manner and had other properties similar to E. coli Lon protease. |
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Significance
Annotations
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