| Range |
100 - 200 ~P (ATP)
|
| Organism |
Eukaryotes |
| Reference |
Michael Lynch and Georgi K. Marinov, The bioenergetic costs of a gene, PNAS 2015 doi: 10.1073/pnas.1514974112 link Supplementary Materials p.5 right column bottom paragraph |
| Primary Source |
Peth A, Nathan JA, Goldberg AL. 2013. The ATP costs and time required to degrade ubiquitinated proteins by the 26S proteasome. J Biol Chem 288 (40):29215-29222. doi: 10.1074/jbc.M113.482570.PubMed ID23965995
|
| Method |
Primary source abstract:"To investigate if the six proteasomal ATPases function independently or in a cyclic manner, as proposed recently, [investigators] used yeast mutants that prevent ATP binding to Rpt3, Rpt5, or Rpt6." |
| Comments |
Supplementary Materials p.5 right column bottom paragraph:"In eukaryotes, protein degradation proceeds by two routes: 1) marking of the proteins by ubiquitination, followed by proteolysis in a proteasome or 2) direct breakdown in a lysosome. Multiple residues on a protein may be covalently linked to ubiquitin, and each such event consumes two high-energy phosphate bonds, i.e., one ATP→AMP conversion (ubiquitin itself is not destroyed but recycled immediately prior to the degradation of the protein). The major cost, however, is associated with the activity of the proteasome, and it is more difficult to quantify: multiple ATPases are involved, and 100 to 200 ATP hydrolyses may typically be required to degrade a single protein [primary source], depending on its length, the difficulty of unfolding it, and other factors." |
| Entered by |
Uri M |
| ID |
112155 |