We are analyzing https://link.springer.com/article/10.1007/s00018-018-2926-5.

Title:
PUM1 and PUM2 exhibit different modes of regulation for SIAH1 that involve cooperativity with NANOS paralogues | Cellular and Molecular Life Sciences
Description:
Pumilio (PUM) proteins are RNA-binding proteins that posttranscriptionally regulate gene expression in many organisms. Their PUF domain recognizes specific PUM-binding elements (PBE) in the 3′ untranslated region of target mRNAs while engaging protein cofactors such as NANOS that repress the expression of target mRNAs through the recruitment of effector complexes. Although the general process whereby PUM recognizes individual mRNAs has been studied extensively, the particulars of the mechanism underlying PUM–NANOS cooperation in mRNA regulation and the functional overlap among PUM and NANOS paralogues in mammals have not been elucidated. Here, using the novel PUM1 and PUM2 mRNA target SIAH1 as a model, we show mechanistic differences between PUM1 and PUM2 and between NANOS1, 2, and 3 paralogues in the regulation of SIAH1. Specifically, unlike PUM2, PUM1 exhibited PBE-independent repression of SIAH1 3′UTR-dependent luciferase expression. Concordantly, the PUF domains of PUM1 and PUM2 showed different EMSA complex formation patterns with SIAH1 3′UTRs. Importantly, we show direct binding of NANOS3, but not NANOS2, to SIAH1 3′UTR, which did not require PBEs or the PUF domain. To the best of our knowledge, this is the first report, showing that an NANOS protein directly binds RNA. Finally, using NANOS1 and NANOS3 constructs carrying mutations identified in infertile patients, we show that these mutations disrupt repression of the SIAH1-luciferase reporter and that the central region in NANOS1 appears to contribute to the regulation of SIAH1. Our findings highlight the mechanistic versatility of the PUM/NANOS machinery in mammalian posttranscriptional regulation.
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Keywords {🔍}

pubmed, article, google, scholar, cas, nanos, pum, central, proteins, cell, pumilio, mrna, human, biol, regulation, drosophila, repression, rna, mol, siah, jaruzelska, rnabinding, protein, experiments, spik, conserved, conducted, life, sciences, puf, target, access, germ, author, privacy, cookies, content, search, manuscript, sajek, maciej, kotecki, blazewicz, domain, mrnas, development, nat, dev, poland, analysis,

Topics {✒️}

kamila kusz-zamelczyk human rna-binding proteins mammalian posttranscriptional regulation month download article/chapter erkut ilaslan rna-binding proteins cchc metal-binding domain p-body purification reveals mirna regulatory system severe oligo-astheno-teratozoospermia cooperative ago2-pum interactions nanos3 gene mutations human pumilio proteins 3′utr regulation pumilio-rna interaction barbara ginter-matuszewska rna-binding full article pdf show direct binding human germ cells zamore pd related subjects cognate rna recognition target rna suppressed pum1 gene human male reproduction weidmann ca engaging protein cofactors check access instant access primary ovarian insufficiency privacy choices/manage cookies testis-specific expression bipartite target sequence drosophila pumilio protein puf family portrait puf proteins ferraz-de-souza premature ovarian insufficiency regulate mrnas independently siah1 3′utr article cellular sperm-oocyte switch pum mrna targets central region de mello mp mutations disrupt repression pumilio proteins nanos-mediated recruitment blazewicz

Questions {❓}

Spassov DS, Jurecic R (2003) The PUF family of RNA-binding proteins: does evolutionarily conserved structure equal conserved function?

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