User:Dmeyer314

Plan for revising Degron page:

What first drew me to this page for revisions is the abundance of claims throughout the text that were unsupported by literature. Additionally, I found most of the current headings/sections were oddly specific and didn't tell the full story about degrons. My current plan for revising this page is to give a more thorough overview of what degrons are, what their functions are in protein turnover and how they can be useful in experimental/biotech environments. If I am able to find more literature that can support/elaborate on what is currently written, then I will incorporate those sections into my revision. Currently, I am searching for that literature as well as reading the other articles I've found in preperation for my update. I anticipate my article's structure being something along the lines of:

section 1: what is a degron (sequence or structure which targets protein for degredation)

section 2: Ubiquitin dependence

-here I'll reference the degron-proteasome connection briefly since proteasome page exists

section 3: Ubiquitin Independence

-IkBa degron example

section 4: utility in experimental biology

-this is where most of the previously written material may appear

https://en.wikipedia.org/wiki/Degron (shown below is my edited form in progress)

A degron is a specific sequence of amino acids in a protein that directs the starting place of degradation. A degron sequence can occur at either the N or C-terminal region: these are called N-degrons or C-degrons respectively. Degradation may be initiated in a ubiquitin-dependent or ubiquitin-independent manor.

A temperature sensitive degron takes advantage of the N-end rule pathway, in which a destabilizing N-terminal residue dramatically decreases the in vivo half-life of a protein. The degron appears a fusion protein of ubiquitin, arginine, and DHFR . DHFR is dihydrofolate reductase, a mouse-derived enzyme that functions in the synthesis of thymine. It is also heat-labile - at a higher temperature of 37°C, becomes slightly unfolded and exposes an internal lysine, the site of poly-ubiquitination. Proteolysis is highly processive, and the protein is degraded by the proteasome. [][The degron can be fused to a gene]=>rephrase because fusing protein sequences to genes isn't what is happening here]]] to produce the corresponding temperature-sensitive protein. It is portable, and can be transferred on a plasmid .

A ligand controllable degron takes advantage of a mutant form of FKBP12 protein that can be controlled using a synthetic ligand. Small molecule Shield1 binds specifically to the degron making it inactive. An inactive degron is no longer recognized by the proteasome, and this [limits/stalls/inhibits] protein degradation. The degron is reactivated when the small molecule is removed by washing the cells and active protein degradation occurs through proteasome mediated proteolysis.

some other things to include:

->Mouse ornithine decarboxylase (MODC) has been fused to fluorophores to reduce half-life

->IkBa degron