Nucleolin Associates with a Subset of the Human Ro Ribonucleoprotein Complexes

Fouraux, Michael A.; Bouvet, Philippe; Verkaart, Sjoerd; Venrooij, Walther J. van; Pruijn, Ger J. M.

doi:10.1016/s0022-2836(02)00518-1

Cited by 62 publications

(64 citation statements)

References 61 publications

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“…Several proteins and RNPs have been reported to interact with this domain in different Y RNAs, including nucleolin, hnRNP K, hnRNP I, and 5S RNP (Fabini et al 2001;Fouraux et al 2002;Hogg and Collins 2007). These interactions do not occur with all Y RNAs (Fabini et al 2000(Fabini et al , 2001Fouraux et al 2002).…”

Section: Functional Analysis Of Hy1 Rna Mutantsmentioning

confidence: 99%

A conserved motif of vertebrate Y RNAs essential for chromosomal DNA replication

Gardiner¹,

Christov²,

Langley³

et al. 2009

RNA

132

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Noncoding Y RNAs are required for the reconstitution of chromosomal DNA replication in late G1 phase template nuclei in a human cell-free system. Y RNA genes are present in all vertebrates and in some isolated nonvertebrates, but the conservation of Y RNA function and key determinants for its function are unknown. Here, we identify a determinant of Y RNA function in DNA replication, which is conserved throughout vertebrate evolution. Vertebrate Y RNAs are able to reconstitute chromosomal DNA replication in the human cell-free DNA replication system, but nonvertebrate Y RNAs are not. A conserved nucleotide sequence motif in the double-stranded stem of vertebrate Y RNAs correlates with Y RNA function. A functional screen of human Y1 RNA mutants identified this conserved motif as an essential determinant for reconstituting DNA replication in vitro. Double-stranded RNA oligonucleotides comprising this RNA motif are sufficient to reconstitute DNA replication, but corresponding DNA or random sequence RNA oligonucleotides are not. In intact cells, wild-type hY1 or the conserved RNA duplex can rescue an inhibition of DNA replication after RNA interference against hY3 RNA. Therefore, we have identified a new RNA motif that is conserved in vertebrate Y RNA evolution, and essential and sufficient for Y RNA function in human chromosomal DNA replication.

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Section: Functional Analysis Of Hy1 Rna Mutantsmentioning

confidence: 99%

A conserved motif of vertebrate Y RNAs essential for chromosomal DNA replication

Gardiner¹,

Christov²,

Langley³

et al. 2009

RNA

132

View full text Add to dashboard Cite

show abstract

“…Several proteins, including nucleolin, the splicing factors Puf60 and hnRNP I, and the interferon-inducible protein IFIT5, all interact with human Ro by binding one or more Y RNAs (Bouffard et al 2000;Fabini et al 2001;Fouraux et al 2002;Hogg and Collins 2007). While these results provide evidence that the multiple Ro/Y RNA complexes found in vertebrate cells may be functionally distinct, the significance of these protein interactions for Ro function remains unknown.…”

Section: Introductionmentioning

confidence: 99%

The zipcode-binding protein ZBP1 influences the subcellular location of the Ro 60-kDa autoantigen and the noncoding Y3 RNA

Sim¹,

Yao²,

Weinberg³

et al. 2011

RNA

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The Ro 60-kDa autoantigen, a ring-shaped RNA-binding protein, traffics between the nucleus and cytoplasm in vertebrate cells. In some vertebrate nuclei, Ro binds misfolded noncoding RNAs and may function in quality control. In the cytoplasm, Ro binds noncoding RNAs called Y RNAs. Y RNA binding blocks a nuclear accumulation signal, retaining Ro in the cytoplasm. Following UV irradiation, this signal becomes accessible, allowing Ro to accumulate in nuclei. To investigate how other cellular components influence the function and subcellular location of Ro, we identified several proteins that copurify with the mouse Ro protein. Here, we report that the zipcode-binding protein ZBP1 influences the subcellular localization of both Ro and the Y3 RNA. Binding of ZBP1 to the Ro/Y3 complex increases after UV irradiation and requires the Y3 RNA. Despite the lack of an identifiable CRM1-dependent export signal, nuclear export of Ro is sensitive to the CRM1 inhibitor leptomycin B. In agreement with a previous report, we find that ZBP1 export is partly dependent on CRM1. Both Ro and Y3 RNA accumulate in nuclei when ZBP1 is depleted. Our data indicate that ZBP1 may function as an adapter to export the Ro/Y3 RNA complex from nuclei.

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“…So far, it has been reported that the RGG box has evolved as an interaction motif to strengthen contacts in RNA-protein complexes (Lengyel et al, 2002) and is considered to have an accessory role in binding the RNA. This has been demonstrated for several RNA-binding proteins such as nucleolin (Ghisolfi et al, 1992;Fouraux et al 2002), fibrillarin (Lapeyre et al, 1990), GAR1 in yeast (Bagni and Lapeyre, 1998) and NSR 1 (Lee et al, 1991). Moreover, in hnRNP A2, RGG repeats are critical for the cellular localization of the protein (Nichols et al, 2000).…”

Section: Structural and Functional Domains Of Fmrpmentioning

confidence: 86%

Molecular Insights into Mental Retardation: Multiple Functions for the Fragile X Mental Retardation Protein?

Zalfa

Bagni

2004

Current Issues in Molecular Biology

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Mental retardation is a frequent cause of intellectual and physical impairment. Several genes associated with mental retardation have been mapped to the X chromosome, among them, there is FMR1. The absence of or mutation in the Fragile Mental Retardation Protein, FMRP, is responsible for the Fragile X syndrome. FMRP is an RNA binding protein that shuttles between the nucleus and the cytoplasm. FMRP binds to several mRNAs including its own mRNA at a sequence region containing a G quartet structure. Some of the candidate downstream genes recently identified encode for synaptic proteins. Neuronal studies indicate that FMRP is located at synapses and loss of FMRP affects synaptic plasticity. At the synapses, FMRP acts as a translational repressor and in particular regulates translation of specific dendritic mRNAs, some of which encode cytoskeletal proteins and signal transduction molecules. This action occurs via a ribonucleoprotein complex that includes a small dendritic non-coding neuronal RNA that determines the specificity of FMRP function via a novel mechanism of translational repression. Since local protein synthesis is required for synaptic development and function, this role of FMRP likely underlies some of the behavioural and developmental symptoms of FRAXA patients. Finally we review recent work on the Drosophila system that connects cytoskeleton remodelling and FMRP function.

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Nucleolin Associates with a Subset of the Human Ro Ribonucleoprotein Complexes

Cited by 62 publications

References 61 publications

A conserved motif of vertebrate Y RNAs essential for chromosomal DNA replication

A conserved motif of vertebrate Y RNAs essential for chromosomal DNA replication

The zipcode-binding protein ZBP1 influences the subcellular location of the Ro 60-kDa autoantigen and the noncoding Y3 RNA

Molecular Insights into Mental Retardation: Multiple Functions for the Fragile X Mental Retardation Protein?

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