A Translation Regulatory Particle Containing theXenopus Oocyte Y Box Protein mRNP3+4

Yurkova, Maria S.; Murray, Mary T.

doi:10.1074/jbc.272.16.10870

Cited by 41 publications

(30 citation statements)

References 58 publications

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“…RlYB2 shared with the Y-box proteins the presence of a highly conserved CSD domain containing two RNP-1 and RNP-2 like motifs that are believed to be important for binding nucleic acids (Sommerville 1999). The presence of numerous residues target for serine/threonine kinases suggested that the RlYB2 activity may be regulated by phosphorylation (Yurkova & Murray 1997). It has been hypothesized that phosphorylation of the C-terminal portion of Ybox proteins facilitates mRNA-protein interactions, while dephosphorylation promotes the release of the bound mRNA (Matsumoto & Wolffe 1998).…”

Section: Discussionmentioning

confidence: 99%

“…The predicted RlYB2 protein had the highly conserved N-terminal CSD (from aa 37 to 85; Figure 2b) with motifs related to RNP-1 and RNP-2 (Auweter et al 2006). Moreover the sequence contains thirteen putative serine/threonine phosphorylation sites (Yurkova & Murray 1997) and two putative nuclear localization signals (from amino acids 157 to 170; Figure 2b) (Nashchekin et al 2006). An arginine-proline rich profile occurred from aa 114 to 317 (Figure 2b).…”

Section: Isolation and Sequence Analysis Of Rlyb2mentioning

confidence: 99%

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Isolation and expression ofRlYB2, a germ cell‐specificY‐boxgene inRana

Marracci

Casola

Bucci

et al. 2008

Italian Journal of Zoology

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Y-box proteins are a highly conserved family of gene expression regulatory factors. During gametogenesis they may play a dual role, as both transcriptional activators of germ cell-specific genes and as translational repressors of stored maternal transcripts. We report the identification of RlYB2, a Y-box homolog gene specifically expressed in the germ cells of green frogs belonging to Rana esculenta complex, a model system characterized by a hybridogenetic gametogenesis. In developing germ cells of the hybrid R. esculenta, arisen by natural cross of the parental species R. ridibunda and R. lessonae, one set of the parental genomes is excluded and the remaining one, first endoreduplicates and then is transmitted to gametes. In situ hybridizations performed on gonadal tissues showed that the RlYB2 transcript was widely expressed in the ooplasm at early stages of oogenesis in both the parental species and hybrids. Interestingly, a hybridization signal, presumably related to RlYB2-like nascent transcripts, was observed in nuclei of stage II oocytes. The presence of RlYB2 mRNA during early oogenesis suggests that this gene may be involved in regulating the transcription and/or translation of maternal mRNAs in this special vertebrate model system.

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Section: Discussionmentioning

confidence: 99%

Section: Isolation and Sequence Analysis Of Rlyb2mentioning

confidence: 99%

Isolation and expression ofRlYB2, a germ cell‐specificY‐boxgene inRana

Marracci

Casola

Bucci

et al. 2008

Italian Journal of Zoology

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“…In addition to being very abundant in the nucleolus, comprising 5 to 10% of the total nucleolar protein, nucleolin was also detected in the cytoplasm (5,8), where its function has only recently been studied (44,45). Like FMRP and the FXR proteins, nucleolin contains an NLS, which enables it to shuttle between the nucleolus and cytoplasm (4,16,26,33).…”

Section: Discussionmentioning

confidence: 99%

Isolation of an FMRP-Associated Messenger Ribonucleoprotein Particle and Identification of Nucleolin and the Fragile X-Related Proteins as Components of the Complex

Ceman

Brown

Warren

1999

Molecular and Cellular Biology

160

144

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The loss of FMR1 expression due to trinucleotide repeat expansion leads to fragile X syndrome, a cause of mental retardation. The encoded protein, FMRP, is a member of a gene family that also contains the fragile X-related proteins, FXR1P and FXR2P. FMRP has been shown to be a nucleocytoplasmic shuttling protein that selectively binds a subset of mRNAs, forms messenger ribonucleoprotein (mRNP) complexes, and associates with translating ribosomes. Here we describe a cell culture system from which we can isolate epitopetagged FMRP along with mRNA, including its own message, and at least six other proteins. We identify two of these proteins as FXR1P and FXR2P by using specific antisera and identify a third protein as nucleolin by using mass spectrometry. The presence of nucleolin is confirmed by both reactivity with a specific antiserum as well as reverse coimmunoprecipitation where antinucleolin antiserum immunoprecipitates endogenous FMRP from both cultured cells and mouse brain. The identification of nucleolin, a known component of other mRNPs, adds a new dimension to the analysis of FMRP function, and the approach described should also allow the identification of the remaining unknown proteins of this FMRP-associated mRNP as well as the other bound mRNAs.Fragile X syndrome is a common form of inherited mental retardation. It is caused by a loss of expression of the FMR1 gene, most often due to an expansion of a CGG repeat in the first exon (reviewed in references 2 and 41). Although this region is untranslated, repeat expansion leads to abnormal methylation and chromatin deacetylation, which results in transcriptional silencing of FMR1 (9,18,28,30,39). The FMR1 gene encodes an approximately 78-kDa protein, FMRP, although multiple isoforms exist due to alternate splicing (1). FMRP contains two hnRNP K-homologous (KH) domains and an RGG box, motifs thought to mediate interactions with mRNA (13). Indeed, FMRP has been shown to bind its own mRNA, homopolymer RNA in vitro, and a subset of brain mRNAs (3,7,35). In addition, FMRP is associated with ribosomes in an RNA-dependent manner (12,40). When lysates were treated with EDTA to dissociate the ribosomal subunits, FMRP was released as a large (greater than 669-kDa) messenger ribonucleoprotein (mRNP) particle containing both poly(A) ϩ mRNA and protein (12,14). Such mRNP complexes are thought to be formed in the cytoplasm after the hnRNP proteins, which associate with the mRNA in transit from the nucleus to the cytoplasm, are released and exchanged for cytoplasmic proteins (11). Some cytoplasmic RNA binding proteins, however, are identical to those found in the nucleus (17). Thus, some proteins seem to remain associated with mRNAs regardless of where the complex is located in the cell. FMRP contains both a functional nuclear localization signal (NLS) and a nuclear export signal (12, 38), and although it is primarily cytoplasmic at steady state, about 5% of the cellular FMRP is nuclear (15). FMRP is therefore believed to shuttle between the nucleus and cytoplasm, compa...

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“…In the cytoplasm, CSD proteins bind mRNAs, affecting their translation fate (21)(22)(23)(24)(25)(26)(27)(28) and extending their lifetime (29).…”

mentioning

confidence: 99%

Poly(A)-binding Protein Positively Affects YB-1 mRNA Translation through Specific Interaction with YB-1 mRNA

Skabkina

Skabkin

Popova

et al. 2003

Journal of Biological Chemistry

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The major protein of cytoplasmic mRNPs from rabbit reticulocytes, YB-1, is a member of an ancient family of proteins containing a common structural feature, coldshock domain. In eukaryotes, this family is represented by multifunctional mRNA/Y-box DNA-binding proteins that control gene expression at different stages. To address possible post-transcriptional regulation of YB-1 gene expression, we examined effects of exogenous 5-and 3-untranslatable region-containing fragments of YB-1 mRNA on its translation and stability in a cell-free system. The addition of the 3 mRNA fragment as well as its subfragment I shut off protein synthesis at the initiation stage without affecting mRNA stability. UV crosslinking revealed four proteins (69, 50, 46, and 44 kDa) that specifically interacted with the 3 mRNA fragment; the inhibitory subfragment I bound two of them, 69-and 50-kDa proteins. We have identified these proteins as PABP (poly(A)-binding protein) (69 kDa) and YB-1 (50 kDa) and demonstrated that titrating out of PABP by poly(A) strongly and specifically inhibits YB-1 mRNA cap ؉ poly(A) ؊ translation in a cell-free system. Thus, PABP is capable of positively affecting YB-1 mRNA translation in a poly(A) tail-independent manner.The evolutionarily conserved family of cold-shock domaincontaining proteins (CSD proteins) 1 is represented in organisms from bacteria to man by multifunctional DNA/RNA-binding proteins (1, 2). In bacteria, some of them known as major cold-shock proteins are responsible for adaptation to growth at low temperatures, and their expression is enormously activated with a temperature decrease (3, 4). In mammalian cells, CSD proteins regulate cell proliferation and differentiation and are involved in cell defense systems (5-11). In the cell nucleus, CSD proteins regulate transcription by interacting with promoters and enhancers of many genes (9, 12-17). They are also involved in DNA replication and repair, as well as in mRNA splicing (5, 18 -20). In the cytoplasm, CSD proteins bind mRNAs, affecting their translation fate (21-28) and extending their lifetime (29).In bacteria, accumulation of major cold-shock proteins at low temperatures was shown to result mainly from strong and selective stabilization of their mRNAs (30, 31). The crucial role of eukaryotic CSD proteins in major cellular events suggests that there is precise regulation of their expression. At present the post-transcriptional control of eukaryotic gene expression is to a large extent attributed to the presence of specific sequences within mRNA 5Ј-and 3Ј-untranslatable regions (UTRs), which serve as targets for binding of certain proteins and complementary RNAs (32, 33). Here, we studied this type of regulation during in vitro synthesis of rabbit p50, a member of the eukaryotic CSD protein family, which is the major protein of reticulocyte mRNPs and is virtually identical to the human Y-box binding protein YB-1. To determine a possible role of YB-1 mRNA UTRs in YB-1 post-transcriptional regulation, we examined effects of exogenous mRNA f...

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A Translation Regulatory Particle Containing theXenopus Oocyte Y Box Protein mRNP3+4

Cited by 41 publications

References 58 publications

Isolation and expression ofRlYB2, a germ cell‐specificY‐boxgene inRana

Isolation and expression ofRlYB2, a germ cell‐specificY‐boxgene inRana

Isolation of an FMRP-Associated Messenger Ribonucleoprotein Particle and Identification of Nucleolin and the Fragile X-Related Proteins as Components of the Complex

Poly(A)-binding Protein Positively Affects YB-1 mRNA Translation through Specific Interaction with YB-1 mRNA

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