scholarly journals Modulation of Aub–TDRD interactions elucidates piRNA amplification and germplasm formation

2020 ◽  
Vol 4 (3) ◽  
pp. e202000912
Author(s):  
Nicholas Vrettos ◽  
Manolis Maragkakis ◽  
Panagiotis Alexiou ◽  
Paraskevi Sgourdou ◽  
Fadia Ibrahim ◽  
...  

Aub guided by piRNAs ensures genome integrity by cleaving retrotransposons, and genome propagation by trapping mRNAs to form the germplasm that instructs germ cell formation. Arginines at the N-terminus of Aub (Aub–NTRs) interact with Tudor and other Tudor domain–containing proteins (TDRDs). Aub–TDRD interactions suppress active retrotransposons via piRNA amplification and form germplasm via generation of Aub–Tudor ribonucleoproteins. Here, we show that Aub–NTRs are dispensable for primary piRNA biogenesis but essential for piRNA amplification and that their symmetric dimethylation is required for germplasm formation and germ cell specification but largely redundant for piRNA amplification.

2018 ◽  
Author(s):  
Elke F. Roovers ◽  
Lucas J.T. Kaaij ◽  
Stefan Redl ◽  
Alfred W. Bronkhorst ◽  
Kay Wiebrands ◽  
...  

SummaryIn recent years, it has become clear that phase separation represents an important class of subcellular compartmentalization. However, relatively little is known about how the formation or disassembly of such compartments is regulated. In zebrafish, the Balbiani body (Bb) and the germ plasm (Gp) are phase-separated structures essential for germ cell specification and home to many germ cell-specific mRNAs and proteins. Throughout development, these structures range from a single large aggregate (Bb), to a dispersed state and back to relatively large assemblies (Gp). Formation of the Bb requires Bucky ball (Buc), a protein with prion-like properties. We found that the multi-tudor domain-containing protein Tdrd6a interacts directly with Buc, affecting its mobility and aggregation properties. Importantly, lack of this regulatory interaction leads to significant defects in germ cell development. Our work presents a new mechanism for how prion-like protein-aggregations can be regulated and highlights the biological relevance of such regulatory events.


2017 ◽  
Vol 65 (3) ◽  
pp. 460-475.e6 ◽  
Author(s):  
Deqing Hu ◽  
Xin Gao ◽  
Kaixiang Cao ◽  
Marc A. Morgan ◽  
Gloria Mas ◽  
...  

2014 ◽  
Vol 4 (1) ◽  
Author(s):  
Antonia A. Dominguez ◽  
H. Rosaria Chiang ◽  
Meena Sukhwani ◽  
Kyle E. Orwig ◽  
Renee A. Reijo Pera

Science ◽  
2007 ◽  
Vol 316 (5823) ◽  
pp. 394-396 ◽  
Author(s):  
K. Hayashi ◽  
S. M. C. de Sousa Lopes ◽  
M. A. Surani

The Lancet ◽  
1977 ◽  
Vol 309 (8007) ◽  
pp. 362-363 ◽  
Author(s):  
P.A. Riley ◽  
P.M. Sutton

Cell Reports ◽  
2017 ◽  
Vol 18 (4) ◽  
pp. 831-839 ◽  
Author(s):  
Dorothy A. Lerit ◽  
Conrad W. Shebelut ◽  
Kristen J. Lawlor ◽  
Nasser M. Rusan ◽  
Elizabeth R. Gavis ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document