English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Specific recognition of  N6 -methyladenosine (m 6 A) in mRNA by RNA-binding proteins containing a YT521-B homology (YTH) domain is important in eukaryotic gene regulation. The  Arabidopsis  YTH domain protein ECT2 is thought to bind to mRNA at URU(m 6 A)Y sites, yet RR(m 6 A)CH is the canonical m 6 A consensus site in all eukaryotes and ECT2 functions require m 6 A-binding activity. Here, we apply iCLIP ( i ndividual nucleotide resolution  c ross l inking and  i mmuno p recipitation) and HyperTRIBE ( t argets of  R NA-binding proteins  i dentified  b y  e diting) to define high-quality target sets of ECT2 and analyze the patterns of enriched sequence motifs around ECT2 crosslink sites. Our analyses show that ECT2 does in fact bind to RR(m 6 A)CH. Pyrimidine-rich motifs are enriched around, but not at m 6 A sites, reflecting a preference for  N6 -adenosine methylation of RRACH/GGAU islands in pyrimidine-rich regions. Such motifs, particularly oligo-U and UNUNU upstream of m 6 A sites, are also implicated in ECT2 binding via its intrinsically disordered region (IDR). Finally, URUAY-type motifs are enriched at ECT2 crosslink sites, but their distinct properties suggest function as sites of competition between binding of ECT2 and as yet unidentified RNA-binding proteins. Our study provides coherence between genetic and molecular studies of m 6 A-YTH function in plants and reveals new insight into the mode of RNA recognition by YTH domain-containing proteins.

Principles of mRNA targeting via the Arabidopsis m 6 A-binding protein ECT2