Analysis of the Microprocessor in Dictyostelium: The Role of RbdB, a dsRNA Binding Protein.
We identified the dsRNA binding protein RbdB as an essential component in miRNA processing in Dictyostelium discoideum. RbdB is a nuclear protein that accumulates, together with Dicer B, in nucleolar foci reminiscent of plant dicing bodies. Disruption of rbdB results in loss of miRNAs and accumulati...
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2016-06-01
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doaj-66f0d031efb645f3868e89fc246b4a112020-11-24T21:42:02ZengPublic Library of Science (PLoS)PLoS Genetics1553-73901553-74042016-06-01126e100605710.1371/journal.pgen.1006057Analysis of the Microprocessor in Dictyostelium: The Role of RbdB, a dsRNA Binding Protein.Doreen MeierJanis KruseJann ButtlarMichael FriedrichFides ZenkBenjamin BoeslerKonrad U FörstnerChristian HammannWolfgang NellenWe identified the dsRNA binding protein RbdB as an essential component in miRNA processing in Dictyostelium discoideum. RbdB is a nuclear protein that accumulates, together with Dicer B, in nucleolar foci reminiscent of plant dicing bodies. Disruption of rbdB results in loss of miRNAs and accumulation of primary miRNAs. The phenotype can be rescued by ectopic expression of RbdB thus allowing for a detailed analysis of domain function. The lack of cytoplasmic dsRBD proteins involved in miRNA processing, suggests that both processing steps take place in the nucleus thus resembling the plant pathway. However, we also find features e.g. in the domain structure of Dicer which suggest similarities to animals. Reduction of miRNAs in the rbdB- strain and their increase in the Argonaute A knock out allowed the definition of new miRNAs one of which appears to belong to a new non-canonical class.http://europepmc.org/articles/PMC4894637?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Doreen Meier Janis Kruse Jann Buttlar Michael Friedrich Fides Zenk Benjamin Boesler Konrad U Förstner Christian Hammann Wolfgang Nellen |
spellingShingle |
Doreen Meier Janis Kruse Jann Buttlar Michael Friedrich Fides Zenk Benjamin Boesler Konrad U Förstner Christian Hammann Wolfgang Nellen Analysis of the Microprocessor in Dictyostelium: The Role of RbdB, a dsRNA Binding Protein. PLoS Genetics |
author_facet |
Doreen Meier Janis Kruse Jann Buttlar Michael Friedrich Fides Zenk Benjamin Boesler Konrad U Förstner Christian Hammann Wolfgang Nellen |
author_sort |
Doreen Meier |
title |
Analysis of the Microprocessor in Dictyostelium: The Role of RbdB, a dsRNA Binding Protein. |
title_short |
Analysis of the Microprocessor in Dictyostelium: The Role of RbdB, a dsRNA Binding Protein. |
title_full |
Analysis of the Microprocessor in Dictyostelium: The Role of RbdB, a dsRNA Binding Protein. |
title_fullStr |
Analysis of the Microprocessor in Dictyostelium: The Role of RbdB, a dsRNA Binding Protein. |
title_full_unstemmed |
Analysis of the Microprocessor in Dictyostelium: The Role of RbdB, a dsRNA Binding Protein. |
title_sort |
analysis of the microprocessor in dictyostelium: the role of rbdb, a dsrna binding protein. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS Genetics |
issn |
1553-7390 1553-7404 |
publishDate |
2016-06-01 |
description |
We identified the dsRNA binding protein RbdB as an essential component in miRNA processing in Dictyostelium discoideum. RbdB is a nuclear protein that accumulates, together with Dicer B, in nucleolar foci reminiscent of plant dicing bodies. Disruption of rbdB results in loss of miRNAs and accumulation of primary miRNAs. The phenotype can be rescued by ectopic expression of RbdB thus allowing for a detailed analysis of domain function. The lack of cytoplasmic dsRBD proteins involved in miRNA processing, suggests that both processing steps take place in the nucleus thus resembling the plant pathway. However, we also find features e.g. in the domain structure of Dicer which suggest similarities to animals. Reduction of miRNAs in the rbdB- strain and their increase in the Argonaute A knock out allowed the definition of new miRNAs one of which appears to belong to a new non-canonical class. |
url |
http://europepmc.org/articles/PMC4894637?pdf=render |
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