YTH protein domain
| YTH protein domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | YTH | ||||||||
| Pfam | PF04146 | ||||||||
| Pfam clan | CL0178 | ||||||||
| InterPro | IPR007275 | ||||||||
| |||||||||
In molecular biology, the
This
Function/mechanism
It has been speculated that in higher order
The YTH domain proteins also serve as readers for the N6-methyladenosine (m6A) mRNA modification by scanning the mRNA to find the modified bases. The YTH domain proteins YTHDF1, YTHDF2, and YTHDF3 can bind to modified bases and the surrounding bases. These YTH proteins recognize RRACH sequences (with the A being the modified m6A, R being a purine, and H being an A, C, or U) and use these sequences as binding sites, allowing them to “read” the modification. The YTHDF2 proteins remove the adenylation on the m6A, destabilizing the RNA transcript and preventing translation. The YTHDF1 proteins have the opposite effect and promote the initiation of translation through their interactions with the 40 S ribosomal subunit.[2]
Structure
The domain is predicted to be a mixed alpha/beta-fold containing four alpha helices and six beta strands.[5] Crystallography studies of these YTH domain proteins show that they have a common hydrophobic region that has been proven to participate in the proteins binding to m6A since mutations in this region decrease binding affinity.[6]
Plant
In