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The N-terminus of FILIA Forms an Atypical KH Domain with a Unique Extension Involved in Interaction with RNA

FILIA is a member of the recently identified oocyte/embryo expressed gene family in eutherian mammals, which is characterized by containing an N-terminal atypical KH domain. Here we report the structure of the N-terminal fragment of FILIA (FILIA-N), which represents the first reported three-dimensio...

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Detalles Bibliográficos
Autores principales: Wang, Juke, Xu, Mengyuan, Zhu, Kai, Li, Lei, Liu, Xinqi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3261892/
https://www.ncbi.nlm.nih.gov/pubmed/22276159
http://dx.doi.org/10.1371/journal.pone.0030209
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author Wang, Juke
Xu, Mengyuan
Zhu, Kai
Li, Lei
Liu, Xinqi
author_facet Wang, Juke
Xu, Mengyuan
Zhu, Kai
Li, Lei
Liu, Xinqi
author_sort Wang, Juke
collection PubMed
description FILIA is a member of the recently identified oocyte/embryo expressed gene family in eutherian mammals, which is characterized by containing an N-terminal atypical KH domain. Here we report the structure of the N-terminal fragment of FILIA (FILIA-N), which represents the first reported three-dimensional structure of a KH domain in the oocyte/embryo expressed gene family of proteins. The structure of FILIA-N revealed a unique N-terminal extension beyond the canonical KH region, which plays important roles in interaction with RNA. By co-incubation with the lysates of mice ovaries, FILIA and FILIA-N could sequester specific RNA components, supporting the critical roles of FILIA in regulation of RNA transcripts during mouse oogenesis and early embryogenesis.
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spelling pubmed-32618922012-01-24 The N-terminus of FILIA Forms an Atypical KH Domain with a Unique Extension Involved in Interaction with RNA Wang, Juke Xu, Mengyuan Zhu, Kai Li, Lei Liu, Xinqi PLoS One Research Article FILIA is a member of the recently identified oocyte/embryo expressed gene family in eutherian mammals, which is characterized by containing an N-terminal atypical KH domain. Here we report the structure of the N-terminal fragment of FILIA (FILIA-N), which represents the first reported three-dimensional structure of a KH domain in the oocyte/embryo expressed gene family of proteins. The structure of FILIA-N revealed a unique N-terminal extension beyond the canonical KH region, which plays important roles in interaction with RNA. By co-incubation with the lysates of mice ovaries, FILIA and FILIA-N could sequester specific RNA components, supporting the critical roles of FILIA in regulation of RNA transcripts during mouse oogenesis and early embryogenesis. Public Library of Science 2012-01-19 /pmc/articles/PMC3261892/ /pubmed/22276159 http://dx.doi.org/10.1371/journal.pone.0030209 Text en Wang et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Wang, Juke
Xu, Mengyuan
Zhu, Kai
Li, Lei
Liu, Xinqi
The N-terminus of FILIA Forms an Atypical KH Domain with a Unique Extension Involved in Interaction with RNA
title The N-terminus of FILIA Forms an Atypical KH Domain with a Unique Extension Involved in Interaction with RNA
title_full The N-terminus of FILIA Forms an Atypical KH Domain with a Unique Extension Involved in Interaction with RNA
title_fullStr The N-terminus of FILIA Forms an Atypical KH Domain with a Unique Extension Involved in Interaction with RNA
title_full_unstemmed The N-terminus of FILIA Forms an Atypical KH Domain with a Unique Extension Involved in Interaction with RNA
title_short The N-terminus of FILIA Forms an Atypical KH Domain with a Unique Extension Involved in Interaction with RNA
title_sort n-terminus of filia forms an atypical kh domain with a unique extension involved in interaction with rna
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3261892/
https://www.ncbi.nlm.nih.gov/pubmed/22276159
http://dx.doi.org/10.1371/journal.pone.0030209
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