Biology:Lon protease family

From HandWiki
Revision as of 03:43, 10 February 2024 by LinXED (talk | contribs) (linkage)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Short description: Family of enzymes
ATP-dependent protease La (LON) domain
PDB 2ane EBI.jpg
crystal structure of n-terminal domain of e.coli lon protease
Identifiers
SymbolLON
PfamPF02190
Pfam clanCL0178
InterProIPR003111
SMARTLON
MEROPSS16
SCOP21zbo / SCOPe / SUPFAM
Lon protease (S16) C-terminal proteolytic domain
Identifiers
SymbolLON
PfamPF05362
Pfam clanCL0329
InterProIPR008269
MEROPSS16
SCOP21rr9 / SCOPe / SUPFAM

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

References

  1. "Proteolytic enzyme | Description, Types, & Functions | Britannica" (in en). https://www.britannica.com/science/proteolytic-enzyme. 
  2. "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. December 1993. doi:10.1073/pnas.90.23.11247. PMID 8248235. Bibcode1993PNAS...9011247W. 
  3. "Maize contains a Lon protease gene that can partially complement a yeast pim1-deletion mutant". Plant Mol. Biol. 37 (1): 141–54. May 1998. doi:10.1023/A:1005912831051. PMID 9620272. 
  4. "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. January 1994. doi:10.1016/S0021-9258(17)42340-4. PMID 8276800. 
  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" (in en). Journal of Microbiology 53 (10): 711–717. doi:10.1007/s12275-015-5417-5. ISSN 1976-3794. PMID 26428922. https://doi.org/10.1007/s12275-015-5417-5. 
  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" (in en). FEBS Open Bio 9 (9): 1536–1551. doi:10.1002/2211-5463.12691. ISSN 2211-5463. PMID 31237118. 

External links

This article incorporates text from the public domain Pfam and InterPro: IPR003111