Lon protease family
ATP-dependent protease La (LON) domain | |||||||||
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crystal structure of n-terminal domain of e.coli lon protease | |||||||||
Identifiers | |||||||||
Symbol | LON | ||||||||
Pfam | PF02190 | ||||||||
Pfam clan | CL0178 | ||||||||
InterPro | IPR003111 | ||||||||
SMART | LON | ||||||||
MEROPS | S16 | ||||||||
SCOP | 1zbo | ||||||||
SUPERFAMILY | 1zbo | ||||||||
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Lon protease (S16) C-terminal proteolytic domain | |||||||||
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Identifiers | |||||||||
Symbol | LON | ||||||||
Pfam | PF05362 | ||||||||
Pfam clan | CL0329 | ||||||||
InterPro | IPR008269 | ||||||||
MEROPS | S16 | ||||||||
SCOP | 1rr9 | ||||||||
SUPERFAMILY | 1rr9 | ||||||||
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In molecular biology, the Lon protease family is a family of proteases. They are found in archaea, bacteria and eukaryotes. Lon proteases are ATP-dependent serine peptidases belonging to the MEROPS peptidase family S16 (lon protease family, clan SJ). In the eukaryotes the majority of the Lon proteases are located in the mitochondrial matrix.[1][2] In yeast, the Lon protease PIM1 is located in the mitochondrial matrix. It is required for mitochondrial function, it is constitutively expressed but is increased after thermal stress, suggesting that PIM1 may play a role in the heat shock response.[3]
See also
References
- ↑ Wang N, Gottesman S, Willingham MC, Gottesman MM, Maurizi MR (December 1993). "A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease". Proc. Natl. Acad. Sci. U.S.A. 90 (23): 11247–51. doi:10.1073/pnas.90.23.11247. PMC 47959. PMID 8248235.
- ↑ Barakat S, Pearce DA, Sherman F, Rapp WD (May 1998). "Maize contains a Lon protease gene that can partially complement a yeast pim1-deletion mutant". Plant Mol. Biol. 37 (1): 141–54. doi:10.1023/A:1005912831051. PMID 9620272.
- ↑ Van Dyck L, Pearce DA, Sherman F (January 1994). "PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae". J. Biol. Chem. 269 (1): 238–42. PMID 8276800.
External links
This article incorporates text from the public domain Pfam and InterPro IPR003111
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