A mitochondrial insertion directs substrate selection and engagement by the protein unfoldase ClpX
Adam DeCosta, Rebecca Barrick, Julia R Kardon · 2026
Read A mitochondrial insertion directs substrate selection and engagement by the protein unfoldase ClpX by Adam DeCosta, Rebecca Barrick, Julia R Kardon (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13671032.txt.
Description
Adam DeCosta, Rebecca Barrick, and Julia Kardon study a tail piece that steers the unfoldase ClpX in mitochondria. Their paper is from two thousand twenty-six. ClpX is a force motor that pulls proteins open so they can be cut or switched on. Its form in mitochondria holds an extra insert on the face that meets substrates, which the bacterial form lacks.
The insert proves key to draw in and switch on ALAS, the first enzyme of heme build, in yeast. In the human pair, it is not needed for guided disposal of ALAS, but it helps grip a plain test substrate. Small tweaks split its grip role from its push on the motor's fuel burn. The insert can thus both fetch a substrate and speed its run through the motor.
Catalog record
| CREATOR | Adam DeCosta, Rebecca Barrick, Julia R Kardon |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 38 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |