Structural studies of the Tudor domain from the Bombyx homolog of Drosophila PAPI: Implication to piRNA biogenesis
Hubbard, P. A.; Pan, X.; McNally, R.; Kirino, Y.; Murali, R.
Show abstract
PIWI proteins and their associated PIWI-interacting RNAs (piRNAs) play crucial roles in proper gametogenesis in animal gonads. Partner of PIWIs (PAPI) is one of the important piRNA biogenesis factors. PAPI contains a Tudor domain and tandem KH domains. The tudor domain specifically recognizes symmetrical-dimethylarginines (sDMAs) on PIWI proteins. BmPAPI, a Bombyx mori homolog of PAPI, is localized at the outer membrane of mitochondria and supports exonucleolytic trimming of piRNA precursors to form mature 3-end of piRNAs. To understand the structural basis of piRNA processing by BmPAPI, we present crystal structures of the apo- and sDMA-liganded Tudor domain of BmPAPI.
Matching journals
The top 10 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Molecular basis for Ras suppressor-1 recruitment to focal adhesions and stabilization of consensus adhesome complex 96%
- Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains 95%
- On the function of TRAP substrate-binding proteins: conformational variation of the sialic acid binding protein SiaP 94%
Similar papers in this journal
Similar papers in this journal
- Mutations affecting the N-terminal domains of SHANK3 point to different pathomechanisms in neurodevelopmental disorders. 94%
- A new perspective on the evolution of the interaction between the Vg/VGLL1-3 proteins and the TEAD transcription factors 94%
- Water stabilizes an alternate turn conformation in horse heart myoglobin 93%
Similar papers in this journal
- Unique structural features of mammalian NEIL2 DNA glycosylase prime its activity for diverse DNA substrates and environments 95%
- Chimeric single α-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology 95%
- Refolding of lid subdomain of SARS-CoV-2 nsp14 upon nsp10 interaction releases exonuclease activity. 93%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.