LONP1: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
 
imported>Neodop
 
(One intermediate revision by one other user not shown)
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Lon protease homolog, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''LONP1'' [[gene]].<ref name="pmid8248235">{{cite journal | vauthors = Wang N, Gottesman S, Willingham MC, Gottesman MM, Maurizi MR | title = A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 90 | issue = 23 | pages = 11247–51 | date = December 1993 | pmid = 8248235 | pmc = 47959 | doi = 10.1073/pnas.90.23.11247 }}</ref><ref name="pmid8119403">{{cite journal | vauthors = Petukhova GV, Grigorenko VG, Lykov IP, Yarovoi SV, Lipkin VM, Gorbalenya AE | title = Cloning and sequence analysis of cDNA for a human homolog of eubacterial ATP-dependent Lon proteases | journal = FEBS Letters | volume = 340 | issue = 1–2 | pages = 25–8 | date = February 1994 | pmid = 8119403 | pmc =  | doi = 10.1016/0014-5793(94)80166-5 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: LONP1 lon peptidase 1, mitochondrial| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9361| accessdate = }}</ref><ref>{{cite journal | vauthors = Pinti M, Gibellini L, Liu Y, Xu S, Lu B, Cossarizza A | title = Mitochondrial Lon protease at the crossroads of oxidative stress, ageing and cancer | journal = Cellular and Molecular Life Sciences | volume = 72 | issue = 24 | pages = 4807–24 | date = December 2015 | pmid = 26363553 | doi = 10.1007/s00018-015-2039-3 }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Structure ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = Lon peptidase 1, mitochondrial
| HGNCid = 9479
| Symbol = LONP1
| AltSymbols =; PIM1; LON; LONP; LonHS; MGC1498; PRSS15; hLON
| OMIM = 605490
| ECnumber = 
| Homologene = 3521
| MGIid = 1921392
| GeneAtlas_image1 = PBB_GE_LONP1_209017_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004176 |text = ATP-dependent peptidase activity}} {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0017111 |text = nucleoside-triphosphatase activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0006510 |text = ATP-dependent proteolysis}} {{GNF_GO|id=GO:0006952 |text = defense response}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 9361
    | Hs_Ensembl = ENSG00000196365
    | Hs_RefseqProtein = NP_004784
    | Hs_RefseqmRNA = NM_004793
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 5642845
    | Hs_GenLoc_end = 5671143
    | Hs_Uniprot = P36776
    | Mm_EntrezGene = 74142
    | Mm_Ensembl = ENSMUSG00000041168
    | Mm_RefseqmRNA = NM_028782
    | Mm_RefseqProtein = NP_083058
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 56299420
    | Mm_GenLoc_end = 56312007
    | Mm_Uniprot = Q56A16
  }}
}}
'''Lon peptidase 1, mitochondrial''', also known as '''LONP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LONP1 lon peptidase 1, mitochondrial| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9361| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encoded a mitochondrial matrix protein that is the subunit of a barrel-shaped homo-oligometric protein complex, the Lon protease.  Lon protease is a member of ATP-dependent proteases ([[AAA proteins|AAA+ proteases]]). Mature and catalytically viable Human Lon protease complex contains a hexameric ring while other formations of complexes have been observed (e.g., heptameric ring in ''Saccharomyces cerevisiae''). A single subunit of Lon protease contains three domains, N-Domain for protein substrate recognition, AAA + module for ATP binding and hydrolysis, and P-domain for protein proteolysis. A similar protease expressed in ''E. coli''  regulates gene expression by targeting specific regulatory proteins for degradation. Lon protease binds a specific sequence in the light and heavy chain promoters of the mitochondrial genome which are involved in regulation of DNA replication and transcription.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a mitochondrial matrix protein in the Lon family of ATP-dependent proteases. A similar E. coli protein regulates gene expression by targeting specific regulatory proteins for degradation. This protein binds a specific sequence in the light and heavy chain promoters of the mitochondrial genome which are involved in regulation of DNA replication and transcription.<ref name="entrez">{{cite web | title = Entrez Gene: LONP1 lon peptidase 1, mitochondrial| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9361| accessdate = }}</ref>
}}


==References==
== Function ==
{{reflist|2}}
 
==Further reading==
Lon protease (LONP1) is a conserved serine peptidase identified from bacteria to eukaryotic cells.<ref>{{cite journal | vauthors = Lu B, Liu T, Crosby JA, Thomas-Wohlever J, Lee I, Suzuki CK | title = The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein that is functionally conserved between yeast and mammals | journal = Gene | volume = 306 | pages = 45–55 | date = March 2003 | pmid = 12657466 | doi = 10.1016/s0378-1119(03)00403-7 }}</ref> In mitochondrial matrix, a majority of damaged proteins is removed via proteolysis led by Lon protease, which is an essential mechanism for mitochondrial protein quality control (PQC).
{{refbegin | 2}}
 
{{PBB_Further_reading
For Lon protease-dependent degradation, protein substrates are first recognized and then unfolded if necessary in an ATP-dependent manner. The substrates are subsequently transferred through the pore of complex and into the proteolytic chamber of complex for degradation. ATP binding to the AAA module of the Lon complex results in a change in Lon conformation into a proteolytically active state. In general, Lon protease interacts with peptide regions(sequences) that are located within the hydrophobic core of substrates and rarely on the surface. These regions can be presented to Lon protease when proteins are damaged and lost their conformation integrity.<ref>{{cite journal | vauthors = Gur E, Sauer RT | title = Recognition of misfolded proteins by Lon, a AAA(+) protease | journal = Genes & Development | volume = 22 | issue = 16 | pages = 2267–77 | date = August 2008 | pmid = 18708584 | doi = 10.1101/gad.1670908 | pmc=2518814}}</ref> In addition to misfolded proteins, several regulatory proteins can be processed by Lon protease by removing a degradable tag before they fully gain their biological functions.<ref>{{cite journal | vauthors = Birghan C, Mundt E, Gorbalenya AE | title = A non-canonical lon proteinase lacking the ATPase domain employs the ser-Lys catalytic dyad to exercise broad control over the life cycle of a double-stranded RNA virus | journal = The EMBO Journal | volume = 19 | issue = 1 | pages = 114–23 | date = January 2000 | pmid = 10619850 | doi = 10.1093/emboj/19.1.114 | pmc=1171783}}</ref>
| citations =  
 
*{{cite journal | author=Lu B, Yadav S, Shah PG, ''et al.'' |title=Roles for the human ATP-dependent Lon protease in mitochondrial DNA maintenance. |journal=J. Biol. Chem. |volume=282 |issue= 24 |pages= 17363-74 |year= 2007 |pmid= 17420247 |doi= 10.1074/jbc.M611540200 }}
LONP1 is also a DNA-binding protein that participates in mtDNA maintenance and gene expression regulation.<ref>{{cite journal | vauthors = Liu T, Lu B, Lee I, Ondrovicová G, Kutejová E, Suzuki CK | title = DNA and RNA binding by the mitochondrial lon protease is regulated by nucleotide and protein substrate | journal = The Journal of Biological Chemistry | volume = 279 | issue = 14 | pages = 13902–10 | date = April 2004 | pmid = 14739292 | doi = 10.1074/jbc.m309642200 }}</ref>  LONP1 degrades mitochondrial transcription factor A ([[TFAM]]) when substrate is modified by post-translational modifications ('''PTM'''s) such as phosphorylation, regulating mtDNA copy number and metabolism to maintain the TFAM/mtDNA ratio necessary to control replication and transcription.<ref>{{cite journal | vauthors = Lu B, Lee J, Nie X, Li M, Morozov YI, Venkatesh S, Bogenhagen DF, Temiakov D, Suzuki CK | title = Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA+ Lon protease | journal = Molecular Cell | volume = 49 | issue = 1 | pages = 121–32 | date = January 2013 | pmid = 23201127 | doi = 10.1016/j.molcel.2012.10.023 | pmc=3586414}}</ref>
*{{cite journal | author=Bota DA, Ngo JK, Davies KJ |title=Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death. |journal=Free Radic. Biol. Med. |volume=38 |issue= 5 |pages= 665-77 |year= 2005 |pmid= 15683722 |doi= 10.1016/j.freeradbiomed.2004.11.017 }}
 
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
== Clinical significance ==
*{{cite journal | author=Liu T, Lu B, Lee I, ''et al.'' |title=DNA and RNA binding by the mitochondrial lon protease is regulated by nucleotide and protein substrate. |journal=J. Biol. Chem. |volume=279 |issue= 14 |pages= 13902-10 |year= 2004 |pmid= 14739292 |doi= 10.1074/jbc.M309642200 }}
 
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
Given the crucial role of LON protease in maintaining the control of mitochondrial function,<ref>{{cite journal | vauthors = Bota DA, Ngo JK, Davies KJ | title = Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death | journal = Free Radical Biology & Medicine | volume = 38 | issue = 5 | pages = 665–77 | date = March 2005 | pmid = 15683722 | doi = 10.1016/j.freeradbiomed.2004.11.017 }}</ref> its dynamics in expression under stress conditions has been found associating with human diseases and aging.<ref>{{cite journal | vauthors = Ngo JK, Pomatto LC, Davies KJ | title = Upregulation of the mitochondrial Lon Protease allows adaptation to acute oxidative stress but dysregulation is associated with chronic stress, disease, and aging | journal = Redox Biology | volume = 1 | pages = 258–64 | date = 9 February 2013 | pmid = 24024159 | doi = 10.1016/j.redox.2013.01.015 | pmc=3757690}}</ref><ref>{{cite journal | vauthors = Hamon MP, Bulteau AL, Friguet B | title = Mitochondrial proteases and protein quality control in ageing and longevity | journal = Ageing Research Reviews | volume = 23 | issue = Pt A | pages = 56–66 | date = September 2015 | pmid = 25578288 | doi = 10.1016/j.arr.2014.12.010 }}</ref> For example, LONP1 expression levels are increased in different tumors and tumor cell lines. Downregulation of LONP1 in some tumor cells causes apoptosis and cell death, indicating a possible addiction of tumor cells to LONP1 function, as occurs with other intracellular proteases associated with cancer.
*{{cite journal | author=Lu B, Liu T, Crosby JA, ''et al.'' |title=The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein that is functionally conserved between yeast and mammals. |journal=Gene |volume=306 |issue= |pages= 45-55 |year= 2003 |pmid= 12657466 |doi= }}
 
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
== See also ==
*{{cite journal | author=Bota DA, Davies KJ |title=Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. |journal=Nat. Cell Biol. |volume=4 |issue= 9 |pages= 674-80 |year= 2002 |pmid= 12198491 |doi= 10.1038/ncb836 }}
*[[Lon protease family]]
*{{cite journal | author=Hori O, Ichinoda F, Tamatani T, ''et al.'' |title=Transmission of cell stress from endoplasmic reticulum to mitochondria: enhanced expression of Lon protease. |journal=J. Cell Biol. |volume=157 |issue= 7 |pages= 1151-60 |year= 2002 |pmid= 12082077 |doi= 10.1083/jcb.200108103 }}
 
*{{cite journal | author=Fu GK, Markovitz DM |title=The human LON protease binds to mitochondrial promoters in a single-stranded, site-specific, strand-specific manner. |journal=Biochemistry |volume=37 |issue= 7 |pages= 1905-9 |year= 1998 |pmid= 9485316 |doi= 10.1021/bi970928c }}
== References ==
*{{cite journal | author=Korenberg JR, Chen XN, Adams MD, Venter JC |title=Toward a cDNA map of the human genome. |journal=Genomics |volume=29 |issue= 2 |pages= 364-70 |year= 1996 |pmid= 8666383 |doi= }}
{{reflist|33em}}
*{{cite journal  | author=Wang N, Gottesman S, Willingham MC, ''et al.'' |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 |year= 1994 |pmid= 8248235 |doi=  }}
 
*{{cite journal  | author=Amerik AYu , Petukhova GV, Grigorenko VG, ''et al.'' |title=Cloning and sequence analysis of cDNA for a human homolog of eubacterial ATP-dependent Lon proteases. |journal=FEBS Lett. |volume=340 |issue= 1-2 |pages= 25-8 |year= 1994 |pmid= 8119403 |doi=  }}
== Further reading ==
*{{cite journal | author=Wang N, Maurizi MR, Emmert-Buck L, Gottesman MM |title=Synthesis, processing, and localization of human Lon protease. |journal=J. Biol. Chem. |volume=269 |issue= 46 |pages= 29308-13 |year= 1994 |pmid= 7961901 |doi=  }}
{{refbegin|33em}}
}}
* {{cite journal | vauthors = Lu B, Yadav S, Shah PG, Liu T, Tian B, Pukszta S, Villaluna N, Kutejová E, Newlon CS, Santos JH, Suzuki CK | title = Roles for the human ATP-dependent Lon protease in mitochondrial DNA maintenance | journal = The Journal of Biological Chemistry | volume = 282 | issue = 24 | pages = 17363–74 | date = June 2007 | pmid = 17420247 | doi = 10.1074/jbc.M611540200 }}
* {{cite journal | vauthors = Bota DA, Ngo JK, Davies KJ | title = Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death | journal = Free Radical Biology & Medicine | volume = 38 | issue = 5 | pages = 665–77 | date = March 2005 | pmid = 15683722 | doi = 10.1016/j.freeradbiomed.2004.11.017 }}
* {{cite journal | vauthors = Liu T, Lu B, Lee I, Ondrovicová G, Kutejová E, Suzuki CK | title = DNA and RNA binding by the mitochondrial lon protease is regulated by nucleotide and protein substrate | journal = The Journal of Biological Chemistry | volume = 279 | issue = 14 | pages = 13902–10 | date = April 2004 | pmid = 14739292 | doi = 10.1074/jbc.M309642200 }}
* {{cite journal | vauthors = Lu B, Liu T, Crosby JA, Thomas-Wohlever J, Lee I, Suzuki CK | title = The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein that is functionally conserved between yeast and mammals | journal = Gene | volume = 306 | issue = | pages = 45–55 | date = March 2003 | pmid = 12657466 | doi = 10.1016/S0378-1119(03)00403-7 }}
* {{cite journal | vauthors = Bota DA, Davies KJ | title = Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism | journal = Nature Cell Biology | volume = 4 | issue = 9 | pages = 674–80 | date = September 2002 | pmid = 12198491 | doi = 10.1038/ncb836 }}
* {{cite journal | vauthors = Hori O, Ichinoda F, Tamatani T, Yamaguchi A, Sato N, Ozawa K, Kitao Y, Miyazaki M, Harding HP, Ron D, Tohyama M, M Stern D, Ogawa S | title = Transmission of cell stress from endoplasmic reticulum to mitochondria: enhanced expression of Lon protease | journal = The Journal of Cell Biology | volume = 157 | issue = 7 | pages = 1151–60 | date = June 2002 | pmid = 12082077 | pmc = 2173558 | doi = 10.1083/jcb.200108103 }}
* {{cite journal | vauthors = Fu GK, Markovitz DM | title = The human LON protease binds to mitochondrial promoters in a single-stranded, site-specific, strand-specific manner | journal = Biochemistry | volume = 37 | issue = 7 | pages = 1905–9 | date = February 1998 | pmid = 9485316 | doi = 10.1021/bi970928c }}
* {{cite journal | vauthors = Korenberg JR, Chen XN, Adams MD, Venter JC | title = Toward a cDNA map of the human genome | journal = Genomics | volume = 29 | issue = 2 | pages = 364–70 | date = September 1995 | pmid = 8666383 | doi = 10.1006/geno.1995.9993 }}
* {{cite journal | vauthors = Wang N, Maurizi MR, Emmert-Buck L, Gottesman MM | title = Synthesis, processing, and localization of human Lon protease | journal = The Journal of Biological Chemistry | volume = 269 | issue = 46 | pages = 29308–13 | date = November 1994 | pmid = 7961901 | doi =  }}
{{refend}}
{{refend}}


{{protein-stub}}
[[Category:EC 3.4.21]]
{{WikiDoc Sources}}
[[Category:Mitochondrial proteins]]

Latest revision as of 16:14, 18 October 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Lon protease homolog, mitochondrial is an enzyme that in humans is encoded by the LONP1 gene.[1][2][3][4]

Structure

This gene encoded a mitochondrial matrix protein that is the subunit of a barrel-shaped homo-oligometric protein complex, the Lon protease. Lon protease is a member of ATP-dependent proteases (AAA+ proteases). Mature and catalytically viable Human Lon protease complex contains a hexameric ring while other formations of complexes have been observed (e.g., heptameric ring in Saccharomyces cerevisiae). A single subunit of Lon protease contains three domains, N-Domain for protein substrate recognition, AAA + module for ATP binding and hydrolysis, and P-domain for protein proteolysis. A similar protease expressed in E. coli regulates gene expression by targeting specific regulatory proteins for degradation. Lon protease binds a specific sequence in the light and heavy chain promoters of the mitochondrial genome which are involved in regulation of DNA replication and transcription.[3]

Function

Lon protease (LONP1) is a conserved serine peptidase identified from bacteria to eukaryotic cells.[5] In mitochondrial matrix, a majority of damaged proteins is removed via proteolysis led by Lon protease, which is an essential mechanism for mitochondrial protein quality control (PQC).

For Lon protease-dependent degradation, protein substrates are first recognized and then unfolded if necessary in an ATP-dependent manner. The substrates are subsequently transferred through the pore of complex and into the proteolytic chamber of complex for degradation. ATP binding to the AAA module of the Lon complex results in a change in Lon conformation into a proteolytically active state. In general, Lon protease interacts with peptide regions(sequences) that are located within the hydrophobic core of substrates and rarely on the surface. These regions can be presented to Lon protease when proteins are damaged and lost their conformation integrity.[6] In addition to misfolded proteins, several regulatory proteins can be processed by Lon protease by removing a degradable tag before they fully gain their biological functions.[7]

LONP1 is also a DNA-binding protein that participates in mtDNA maintenance and gene expression regulation.[8] LONP1 degrades mitochondrial transcription factor A (TFAM) when substrate is modified by post-translational modifications (PTMs) such as phosphorylation, regulating mtDNA copy number and metabolism to maintain the TFAM/mtDNA ratio necessary to control replication and transcription.[9]

Clinical significance

Given the crucial role of LON protease in maintaining the control of mitochondrial function,[10] its dynamics in expression under stress conditions has been found associating with human diseases and aging.[11][12] For example, LONP1 expression levels are increased in different tumors and tumor cell lines. Downregulation of LONP1 in some tumor cells causes apoptosis and cell death, indicating a possible addiction of tumor cells to LONP1 function, as occurs with other intracellular proteases associated with cancer.

See also

References

  1. ↑ 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". Proceedings of the National Academy of Sciences of the United States of America. 90 (23): 11247–51. doi:10.1073/pnas.90.23.11247. PMC 47959. PMID 8248235.
  2. ↑ Petukhova GV, Grigorenko VG, Lykov IP, Yarovoi SV, Lipkin VM, Gorbalenya AE (February 1994). "Cloning and sequence analysis of cDNA for a human homolog of eubacterial ATP-dependent Lon proteases". FEBS Letters. 340 (1–2): 25–8. doi:10.1016/0014-5793(94)80166-5. PMID 8119403.
  3. ↑ 3.0 3.1 "Entrez Gene: LONP1 lon peptidase 1, mitochondrial".
  4. ↑ Pinti M, Gibellini L, Liu Y, Xu S, Lu B, Cossarizza A (December 2015). "Mitochondrial Lon protease at the crossroads of oxidative stress, ageing and cancer". Cellular and Molecular Life Sciences. 72 (24): 4807–24. doi:10.1007/s00018-015-2039-3. PMID 26363553.
  5. ↑ Lu B, Liu T, Crosby JA, Thomas-Wohlever J, Lee I, Suzuki CK (March 2003). "The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein that is functionally conserved between yeast and mammals". Gene. 306: 45–55. doi:10.1016/s0378-1119(03)00403-7. PMID 12657466.
  6. ↑ Gur E, Sauer RT (August 2008). "Recognition of misfolded proteins by Lon, a AAA(+) protease". Genes & Development. 22 (16): 2267–77. doi:10.1101/gad.1670908. PMC 2518814. PMID 18708584.
  7. ↑ Birghan C, Mundt E, Gorbalenya AE (January 2000). "A non-canonical lon proteinase lacking the ATPase domain employs the ser-Lys catalytic dyad to exercise broad control over the life cycle of a double-stranded RNA virus". The EMBO Journal. 19 (1): 114–23. doi:10.1093/emboj/19.1.114. PMC 1171783. PMID 10619850.
  8. ↑ Liu T, Lu B, Lee I, Ondrovicová G, Kutejová E, Suzuki CK (April 2004). "DNA and RNA binding by the mitochondrial lon protease is regulated by nucleotide and protein substrate". The Journal of Biological Chemistry. 279 (14): 13902–10. doi:10.1074/jbc.m309642200. PMID 14739292.
  9. ↑ Lu B, Lee J, Nie X, Li M, Morozov YI, Venkatesh S, Bogenhagen DF, Temiakov D, Suzuki CK (January 2013). "Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA+ Lon protease". Molecular Cell. 49 (1): 121–32. doi:10.1016/j.molcel.2012.10.023. PMC 3586414. PMID 23201127.
  10. ↑ Bota DA, Ngo JK, Davies KJ (March 2005). "Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death". Free Radical Biology & Medicine. 38 (5): 665–77. doi:10.1016/j.freeradbiomed.2004.11.017. PMID 15683722.
  11. ↑ Ngo JK, Pomatto LC, Davies KJ (9 February 2013). "Upregulation of the mitochondrial Lon Protease allows adaptation to acute oxidative stress but dysregulation is associated with chronic stress, disease, and aging". Redox Biology. 1: 258–64. doi:10.1016/j.redox.2013.01.015. PMC 3757690. PMID 24024159.
  12. ↑ Hamon MP, Bulteau AL, Friguet B (September 2015). "Mitochondrial proteases and protein quality control in ageing and longevity". Ageing Research Reviews. 23 (Pt A): 56–66. doi:10.1016/j.arr.2014.12.010. PMID 25578288.

Further reading

  • Lu B, Yadav S, Shah PG, Liu T, Tian B, Pukszta S, Villaluna N, Kutejová E, Newlon CS, Santos JH, Suzuki CK (June 2007). "Roles for the human ATP-dependent Lon protease in mitochondrial DNA maintenance". The Journal of Biological Chemistry. 282 (24): 17363–74. doi:10.1074/jbc.M611540200. PMID 17420247.
  • Bota DA, Ngo JK, Davies KJ (March 2005). "Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death". Free Radical Biology & Medicine. 38 (5): 665–77. doi:10.1016/j.freeradbiomed.2004.11.017. PMID 15683722.
  • Liu T, Lu B, Lee I, Ondrovicová G, Kutejová E, Suzuki CK (April 2004). "DNA and RNA binding by the mitochondrial lon protease is regulated by nucleotide and protein substrate". The Journal of Biological Chemistry. 279 (14): 13902–10. doi:10.1074/jbc.M309642200. PMID 14739292.
  • Lu B, Liu T, Crosby JA, Thomas-Wohlever J, Lee I, Suzuki CK (March 2003). "The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein that is functionally conserved between yeast and mammals". Gene. 306: 45–55. doi:10.1016/S0378-1119(03)00403-7. PMID 12657466.
  • Bota DA, Davies KJ (September 2002). "Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism". Nature Cell Biology. 4 (9): 674–80. doi:10.1038/ncb836. PMID 12198491.
  • Hori O, Ichinoda F, Tamatani T, Yamaguchi A, Sato N, Ozawa K, Kitao Y, Miyazaki M, Harding HP, Ron D, Tohyama M, M Stern D, Ogawa S (June 2002). "Transmission of cell stress from endoplasmic reticulum to mitochondria: enhanced expression of Lon protease". The Journal of Cell Biology. 157 (7): 1151–60. doi:10.1083/jcb.200108103. PMC 2173558. PMID 12082077.
  • Fu GK, Markovitz DM (February 1998). "The human LON protease binds to mitochondrial promoters in a single-stranded, site-specific, strand-specific manner". Biochemistry. 37 (7): 1905–9. doi:10.1021/bi970928c. PMID 9485316.
  • Korenberg JR, Chen XN, Adams MD, Venter JC (September 1995). "Toward a cDNA map of the human genome". Genomics. 29 (2): 364–70. doi:10.1006/geno.1995.9993. PMID 8666383.
  • Wang N, Maurizi MR, Emmert-Buck L, Gottesman MM (November 1994). "Synthesis, processing, and localization of human Lon protease". The Journal of Biological Chemistry. 269 (46): 29308–13. PMID 7961901.
Retrieved from "https://www.wikidoc.org/index.php?title=LONP1&oldid=1529842"