A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease.
Open Access
- 1 December 1993
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 90 (23) , 11247-11251
- https://doi.org/10.1073/pnas.90.23.11247
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.Keywords
This publication has 38 references indexed in Scilit:
- The lonD gene is homologous to the lon gene encoding an ATP-dependent protease and is essential for the development of Myxococcus xanthusJournal of Bacteriology, 1993
- 3,400 new expressed sequence tags identify diversity of transcripts in human brainNature Genetics, 1993
- Cloning and nucleotide sequence of the Myxococcus xanthus lon gene: indispensability of lon for vegetative growthJournal of Bacteriology, 1993
- Regulation by proteolysis: energy-dependent proteases and their targets.1992
- Protease La, the lon gene product, cleaves specific fluorogenic peptides in an ATP-dependent reaction.Journal of Biological Chemistry, 1985
- Demonstration of an ATP-dependent, vanadate-sensitive endoprotease in the matrix of rat liver mitochondria.Journal of Biological Chemistry, 1982
- Liver mitochondria contain an ATP-dependent, vanadate-sensitive pathway for the degradation of proteins.Proceedings of the National Academy of Sciences, 1982
- The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La.Proceedings of the National Academy of Sciences, 1981
- ATP hydrolysis-dependent protease activity of the lon (capR) protein of Escherichia coli K-12.Proceedings of the National Academy of Sciences, 1981
- DNA sequencing with chain-terminating inhibitorsProceedings of the National Academy of Sciences, 1977