Lon protease family explained

Symbol:	LON
ATP-dependent protease La (LON) domain
Pfam:	PF02190
Pfam Clan:	CL0178
Interpro:	IPR003111
Smart:	LON
Merops:	S16
Scop:	1zbo

Symbol:	LON
Lon protease (S16) C-terminal proteolytic domain
Pfam:	PF05362
Pfam Clan:	CL0329
Interpro:	IPR008269
Merops:	S16
Scop:	1rr9

In molecular biology, the Lon protease family is a family of enzymes that break peptide bonds in proteins resulting in smaller peptides or amino acids.^[1] 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.^{[2] [3]} 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.^[4] Lon proteases have two specific subfamilies: LonA and LonB, differentiated by the number of AAA+ domains found in the protein.^{[5] [6]}

See also

• LONP1

External links

• MEROPS family S16

Notes and References

1. Web site: Proteolytic enzyme Description, Types, & Functions Britannica . 2022-12-05 . www.britannica.com . en.
2. 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 . 1993PNAS...9011247W . 10.1073/pnas.90.23.11247 . 47959 . 8248235 . free.
3. 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 . 10.1023/A:1005912831051 . 9620272 . 94168.
4. 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 . 10.1016/S0021-9258(17)42340-4 . 8276800 . free.
5. An . Young Jun . Na . Jung-Hyun . Kim . Myung-Il . Cha . Sun-Shin . 2015-10-01 . Structural basis for the ATP-independent proteolytic activity of LonB proteases and reclassification of their AAA+ modules . Journal of Microbiology . en . 53 . 10 . 711–717 . 10.1007/s12275-015-5417-5 . 26428922 . 14281538 . 1976-3794.
6. Rotanova . Tatyana V. . Andrianova . Anna G. . Kudzhaev . Arsen M. . Li . Mi . Botos . Istvan . Wlodawer . Alexander . Gustchina . Alla . September 2019 . New insights into structural and functional relationships between LonA proteases and ClpB chaperones . FEBS Open Bio . en . 9 . 9 . 1536–1551 . 10.1002/2211-5463.12691 . 2211-5463 . 6722904 . 31237118.