| Range |
~50 %
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Gur E, Sauer RT. Degrons in protein substrates program the speed and operating efficiency of the AAA+ Lon proteolytic machine. Proc Natl Acad Sci U S A. 2009 Nov 3 106(44):18503-8. doi: 10.1073/pnas.0910392106. p.18503 left column 3rd paragraphPubMed ID19841274
|
| Primary Source |
[6] Chung CH, Goldberg AL (1981) The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La. Proc Natl Acad Sci USA 78: 4931–4935.PubMed ID6458037
|
| Comments |
p.18503 left column 3rd paragraph:"Lon degrades damaged proteins in bacteria and eukaryotic organelles (refs 4–6). For example, Lon degrades approximately 50% of the misfolded proteome in Escherichia coli (primary source 6). Functional Lon is a homohexamer. Each subunit consists of an N domain, an AAA+ ATPase domain that provides mechanical power, and a peptidase domain (refs 7–8). Lon's ability to distinguish misfolded variants from correctly folded proteins depends on recognition of degradation tags rich in aromatic and hydrophobic residues, which tend to be hidden in the core of native proteins but become accessible upon denaturation (ref 9). Lon also possesses an unfoldase activity, and some substrates are native proteins with accessible degrons (refs 9–13)." Degron=a specific sequence of amino acids in a protein that directs the starting place of degradation [wikipedia]. |
| Entered by |
Uri M |
| ID |
111875 |