PMID:8248235

Citation	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.
Links	PubMed PMC47959
Keywords	ATP-Dependent Proteases; Amino Acid Sequence; Base Sequence; Blotting, Western; Cloning, Molecular; DNA, Complementary/genetics; Escherichia coli Proteins; Genes; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Humans; Mitochondria/enzymology; Molecular Sequence Data; Mutagenesis, Site-Directed; Protease La; Sequence Alignment; Sequence Homology, Amino Acid; Serine Endopeptidases/chemistry; Serine Endopeptidases/genetics; Serine Endopeptidases/metabolism; Structure-Activity Relationship; Tissue Distribution
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Gene product	Qualifier	GO ID	GO term name	Evidence Code	with/from	Aspect	Notes	Status
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