scholarly journals Protein Argonaute-1

2020 ◽  
Author(s):  
Keyword(s):  
Plants ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 267
Author(s):  
Axel J. Giudicatti ◽  
Ariel H. Tomassi ◽  
Pablo A. Manavella ◽  
Agustin L. Arce

MicroRNAs are small regulatory RNAs involved in several processes in plants ranging from development and stress responses to defense against pathogens. In order to accomplish their molecular functions, miRNAs are methylated and loaded into one ARGONAUTE (AGO) protein, commonly known as AGO1, to stabilize and protect the molecule and to assemble a functional RNA-induced silencing complex (RISC). A specific machinery controls miRNA turnover to ensure the silencing release of targeted-genes in given circumstances. The trimming and tailing of miRNAs are fundamental modifications related to their turnover and, hence, to their action. In order to gain a better understanding of these modifications, we analyzed Arabidopsis thaliana small RNA sequencing data from a diversity of mutants, related to miRNA biogenesis, action, and turnover, and from different cellular fractions and immunoprecipitations. Besides confirming the effects of known players in these pathways, we found increased trimming and tailing in miRNA biogenesis mutants. More importantly, our analysis allowed us to reveal the importance of ARGONAUTE 1 (AGO1) loading, slicing activity, and cellular localization in trimming and tailing of miRNAs.


2018 ◽  
Vol 44 (3) ◽  
pp. 348-361.e7 ◽  
Author(s):  
Chang Liu ◽  
Ying Xin ◽  
Le Xu ◽  
Zhaokui Cai ◽  
Yuanchao Xue ◽  
...  

Development ◽  
2007 ◽  
Vol 134 (23) ◽  
pp. 4265-4272 ◽  
Author(s):  
L. Yang ◽  
D. Chen ◽  
R. Duan ◽  
L. Xia ◽  
J. Wang ◽  
...  

2018 ◽  
Vol 115 (28) ◽  
pp. E6659-E6667 ◽  
Author(s):  
Xiaoyan Wang ◽  
Yuan Wang ◽  
Yongchao Dou ◽  
Lu Chen ◽  
Junli Wang ◽  
...  

The 3′ end methylation catalyzed by HUA Enhancer 1 (HEN1) is a crucial step of small RNA stabilization in plants, yet how unmethylated small RNAs undergo degradation remains largely unknown. Using a reverse genetic approach, we here show that Atrimmer 2 (ATRM2), a DEDDy-type 3′ to 5′ exoribonuclease, acts in the degradation of unmethylated miRNAs and miRNA*s in Arabidopsis. Loss-of-function mutations in ATRM2 partially suppress the morphological defects caused by HEN1 malfunction, with restored levels of a subset of miRNAs and receded expression of corresponding miRNA targets. Dysfunction of ATRM2 has negligible effect on miRNA trimming, and further increase the fertility of hen1 heso1 urt1, a mutant with an almost complete abolishment of miRNA uridylation, indicating that ATRM2 may neither be involved in 3′ to 5′ trimming nor be the enzyme that specifically degrades uridylated miRNAs. Notably, the fold changes of miRNAs and their corresponding miRNA*s were significantly correlated in hen1 atrm2 versus hen1. Unexpectedly, we observed a marked increase of 3′ to 5′ trimming of several miRNA*s but not miRNAs in ATRM2 compromised backgrounds. These data suggest an action of ATRM2 on miRNA/miRNA* duplexes, and the existence of an unknown exoribonuclease for specific trimming of miRNA*. This asymmetric effect on miRNA/miRNA* is likely related to Argonaute (AGO) proteins, which can distinguish miRNAs from miRNA*s. Finally, we show that ATRM2 colocalizes and physically interacts with Argonaute 1 (AGO1). Taken together, our results suggest that ATRM2 may be involved in the surveillance of unmethylated miRNA/miRNA* duplexes during the initiation step of RNA-induced silencing complex assembly.


Cell Reports ◽  
2013 ◽  
Vol 3 (6) ◽  
pp. 1901-1909 ◽  
Author(s):  
Christopher R. Faehnle ◽  
Elad Elkayam ◽  
Astrid D. Haase ◽  
Gregory J. Hannon ◽  
Leemor Joshua-Tor
Keyword(s):  

2017 ◽  
Vol 01 (01) ◽  
Author(s):  
Mondal T ◽  
Pal D ◽  
Bhadra MP ◽  
Bhadra U
Keyword(s):  

2017 ◽  
Vol 36 (11) ◽  
pp. 1641-1642 ◽  
Author(s):  
Éva Várallyay ◽  
Anna Válóczi ◽  
Ákos Ágyi ◽  
József Burgyán ◽  
Zoltán Havelda
Keyword(s):  

2014 ◽  
Vol 65 (22) ◽  
pp. 6293-6299 ◽  
Author(s):  
Chaogang Shao ◽  
Ai-wen Dong ◽  
Xiaoxia Ma ◽  
Yijun Meng

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