Lon protease family

{{Short description|Family of enzymes}}

{{technical|date=February 2012}}

{{Infobox protein family

| Symbol = LON

| Name = ATP-dependent protease La (LON) domain

| image = PDB 2ane EBI.jpg

| width =

| caption = crystal structure of n-terminal domain of e.coli lon protease

| Pfam = PF02190

| Pfam_clan = CL0178

| InterPro = IPR003111

| SMART = LON

| PROSITE =

| MEROPS = S16

| SCOP = 1zbo

| TCDB =

| OPM family =

| OPM protein =

| CAZy =

| CDD =

}}

{{Infobox protein family

| Symbol = LON

| Name = Lon protease (S16) C-terminal proteolytic domain

| image =

| width =

| caption =

| Pfam = PF05362

| Pfam_clan = CL0329

| InterPro = IPR008269

| SMART =

| PROSITE =

| MEROPS = S16

| SCOP = 1rr9

| TCDB =

| OPM family =

| OPM protein =

| CAZy =

| CDD =

}}

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.{{Cite web |title=Proteolytic enzyme {{!}} Description, Types, & Functions {{!}} Britannica |url=https://www.britannica.com/science/proteolytic-enzyme |access-date=2022-12-05 |website=www.britannica.com |language=en}} 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.{{cite journal |vauthors=Wang N, Gottesman S, Willingham MC, Gottesman MM, Maurizi MR |date=December 1993 |title=A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue=23 |pages=11247–51 |bibcode=1993PNAS...9011247W |doi=10.1073/pnas.90.23.11247 |pmc=47959 |pmid=8248235 |doi-access=free}}{{cite journal |vauthors=Barakat S, Pearce DA, Sherman F, Rapp WD |date=May 1998 |title=Maize contains a Lon protease gene that can partially complement a yeast pim1-deletion mutant |journal=Plant Mol. Biol. |volume=37 |issue=1 |pages=141–54 |doi=10.1023/A:1005912831051 |pmid=9620272 |s2cid=94168}} 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.{{cite journal |vauthors=Van Dyck L, Pearce DA, Sherman F |date=January 1994 |title=PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae |journal=J. Biol. Chem. |volume=269 |issue=1 |pages=238–42 |doi=10.1016/S0021-9258(17)42340-4 |pmid=8276800 |doi-access=free}} Lon proteases have two specific subfamilies: LonA and LonB, differentiated by the number of AAA+ domains found in the protein.{{Cite journal |last1=An |first1=Young Jun |last2=Na |first2=Jung-Hyun |last3=Kim |first3=Myung-Il |last4=Cha |first4=Sun-Shin |date=2015-10-01 |title=Structural basis for the ATP-independent proteolytic activity of LonB proteases and reclassification of their AAA+ modules |url=https://doi.org/10.1007/s12275-015-5417-5 |journal=Journal of Microbiology |language=en |volume=53 |issue=10 |pages=711–717 |doi=10.1007/s12275-015-5417-5 |pmid=26428922 |s2cid=14281538 |issn=1976-3794|url-access=subscription }}{{Cite journal |last1=Rotanova |first1=Tatyana V. |last2=Andrianova |first2=Anna G. |last3=Kudzhaev |first3=Arsen M. |last4=Li |first4=Mi |last5=Botos |first5=Istvan |last6=Wlodawer |first6=Alexander |last7=Gustchina |first7=Alla |date=September 2019 |title=New insights into structural and functional relationships between LonA proteases and ClpB chaperones |journal=FEBS Open Bio |language=en |volume=9 |issue=9 |pages=1536–1551 |doi=10.1002/2211-5463.12691 |issn=2211-5463 |pmc=6722904 |pmid=31237118}}