Abstract
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.
Highlights
RNA binding proteins (RBPs) play critical roles in germline and early embryonic development in model organisms by regulating RNA splicing, RNA subcellular localization, mRNA stability and translation [1,2,3,4]
FILIA is a member of a recently identified oocyte/embryo expressed family whose members are characterized by an atypical K homology (KH) domain
Khdc1a/Ndg1 was originally described as a downstream target of Nur77, a nuclear orphan steroid receptor in T-cells, and may be involved in apoptosis [31,35]
Summary
RNA binding proteins (RBPs) play critical roles in germline and early embryonic development in model organisms by regulating RNA splicing, RNA subcellular localization, mRNA stability and translation [1,2,3,4]. It is implied that KH domain containing proteins play critical roles in gene expression by regulating premRNA splicing, and by their involvement in polyadenylation, translation and RNA degradation. Filia has been classified into a new oocyte/embryo expressed gene family in eutherian mammals, along with khdc, dppa, and floped [31]. Proteins in this gene family are characterized by an atypical N-terminal KH domain and their sequence varies greatly beyond the KH domain. The structure of FILIA-N shows several features unique to FILIA and the probable function of the N-terminal extension prior to the KH domain was studied with regard to RNA binding. FILIA-N forms a stable dimer in both crystals and solution with high affinity, which is distinct from canonical KH domains
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