Heterogeneous nuclear ribonucleoprotein D0B is a sequence-specificDNA-binding protein

Tolnay, Máté; Vereshchagina, Lyudmila A.; Tsokos, George C.

doi:10.1042/bj3380417

Cited by 38 publications

(7 citation statements)

References 34 publications

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“…Regardless of their possible modifications, these proteins are differentially expressed during HFK18 differentiation. Both proteins are RNA- and DNA-binding proteins and could function as transcription factors or repressors for mammalian promoters (60–63, 81, 82) and for an EBV C promoter (83). Consistent with these findings (62, 63), our data suggest that the binding of hnRNP D0B and hnRNP A/B to the HPV18 late promoter may regulate the level of the DNA replication-dependent promoter.…”

Section: Discussionmentioning

confidence: 99%

Viral DNA Replication Orientation and hnRNPs Regulate Transcription of the Human Papillomavirus 18 Late Promoter

Wang

Liu

Ge³

et al. 2017

mBio

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The life cycle of human papillomaviruses (HPVs) is tightly linked to keratinocyte differentiation. Although expression of viral early genes is initiated immediately upon virus infection of undifferentiated basal cells, viral DNA amplification and late gene expression occur only in the mid to upper strata of the keratinocytes undergoing terminal differentiation. In this report, we show that the relative activity of HPV18 TATA-less late promoter P811 depends on its orientation relative to that of the origin (Ori) of viral DNA replication and is sensitive to the eukaryotic DNA polymerase inhibitor aphidicolin. Additionally, transfected 70-nucleotide (nt)-long single-strand DNA oligonucleotides that are homologous to the region near Ori induce late promoter activity. We also found that promoter activation in raft cultures leads to production of the late promoter-associated, sense-strand transcription initiation RNAs (tiRNAs) and splice-site small RNAs (spliRNAs). Finally, a cis-acting AAGTATGCA core element that functions as a repressor to the promoter was identified. This element interacts with hnRNP D0B and hnRNP A/B factors. Point mutations in the core prevented binding of hnRNPs and increased the promoter activity. Confirming this result, knocking down the expression of both hnRNPs in keratinocytes led to increased promoter activity. Taking the data together, our study revealed the mechanism of how the HPV18 late promoter is regulated by DNA replication and host factors.

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Section: Discussionmentioning

confidence: 99%

Viral DNA Replication Orientation and hnRNPs Regulate Transcription of the Human Papillomavirus 18 Late Promoter

Wang

Liu

Ge³

et al. 2017

mBio

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“…This factor activates the c-myc promoter (37,38). Since then, a number of genes have been shown to be regulated by hnRNP proteins, for example, osteocalcin (39), CR2 (23)(24)(25), CD28 (26), CD43 (40), AP-endonuclease 1 (41), C/EBP R (42), rat spi2 (43), LMP/TAP gene cluster in major histocompatibility complex class II (44), and Bax (27). The present study adds the KLF2 gene to this list.…”

Section: Discussionmentioning

confidence: 99%

“…Identical results were also obtained by subjecting the protein fractions to mass spectroscopy directly after elution. Several transcriptional factors including CArG binding factor (CBF) (20)(21)(22), heterogeneous nuclear ribonucleoprotein D (hnRNP-D) (23)(24)(25)(26), heterogeneous nuclear ribonucleoprotein U (hnRNP-U) (27), P-300/CBP associated factor (PCAF) (28), a component of SWI/SNF complex (29), and cAMP response element binding protein (CREB) (30) were identified (Table 1). Additionally glucose-regulated protein-78 FIGURE 4: Electrophoretic mobility supershift assays with Mef-2, Sp1, CDP, TAFII, and TAF11B antibodies.…”

Section: Selection Of Macrophage Cell Line Wr 19m1 For Identificatiomentioning

confidence: 99%

Kruppel-like factor 2 Transcriptional Regulation Involves Heterogeneous Nuclear Ribonucleoproteins and Acetyltransferases

Ahmad

Lingrel

2005

Biochemistry

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Kruppel-like factor 2 (KLF2) is expressed in several cell types, and knockout animals have shown that KLF2 gene regulation is involved in multiple biological processes. These include maintaining T-cells in the quiescent state, preventing preadipocytes from differentiating into mature adipocytes, stabilizing blood vessel walls through endothelial cell function, and advancing the later stages of lung development. Defining the regulation of KLF2 expression is important to understand these diverse functions. Promoter analysis of KLF2 has revealed that a region between -138 and -111 base pairs is required for its transcription, and this nucleotide sequence occurs in a region that is highly conserved in evolution. The present study was carried out to identify transcription factors that bind to this region of the KLF2 promoter. Nuclear factors were enriched by DNA affinity chromatography using the conserved nucleotide sequence of the KLF2 promoter. Mass spectrometry analysis of the proteins eluted from the affinity matrix identified several proteins, including glucose regulated protein-78 kDa (GRP-78), heterogeneous nuclear ribonucleoprotein (hnRNP)-U, hnRNP-D, CArG binding factor (CBF), P300/CBP associated factor (PCAF), cAMP response element binding protein (CREB) and SWI/SNF. The binding of these proteins to the highly conserved region of the KLF2 promoter element was tested by electrophoretic mobility supershift assays and chromatin immunoprecipitation analysis. These procedures confirmed that hnRNP-U, hnRNP-D, PCAF, and P-300 bind to the KLF2 promoter. Transactivation experiments demonstrated that these proteins are important for regulating KLF2 transcription. Of special interest is the role of hnRNPs in the transcription of the KLF2 gene.

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“…However, the varying affinity for RNA versus DNA and double-stranded DNA (dsDNA) versus ssDNA suggests that binding properties of a RRM are specific rather than ‘generic’ for DNA. Even closely related hnRNPs, such as AUF1 and hnRNP DOB, both of which have homologous RRMs that bind AU-rich RNAs, have markedly different affinities for DNA (40). With TIAR, the nearly 6-fold higher affinity for DNA over RNA, however, was surprising since RRMs in general bind preferably to RNA (39).…”

Section: Discussionmentioning

confidence: 99%

Novel DNA-binding properties of the RNA-binding protein TIAR

Suswam¹

2005

Nucleic Acids Research

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TIA-1 related protein binds avidly to uridine-rich elements in mRNA and pre-mRNAs of a wide range of genes, including interleukin (IL)-8 and vascular endothelial growth factor (VEGF). The protein has diverse regulatory roles, which in part depend on the locus of binding within the transcript, including translational control, splicing and apoptosis. Here, we observed selective and potent inhibition of TIAR–RNP complex formation with IL-8 and VEGF 3′-untranslated regions (3′-UTRs) using thymidine-rich deoxyoligonucleotide (ODN) sequences derived from the VEFG 3′-UTR. We show by ultraviolet crosslinking and electrophoretic mobility shift assays that TIAR can bind directly to single-stranded, thymidine-rich ODNs but not to double-stranded ODNs containing the same sequence. TIAR had a nearly 6-fold greater affinity for DNA than RNA (Kdapp=1.6×10−9M versus 9.4 × 10−9 M). Truncation of TIAR indicated that the high affinity DNA-binding site overlaps with the RNA-binding site involving RNA recognition motif 2 (RRM2). However, RRM1 alone could also bind to DNA. Finally, we show that TIAR can be displaced from single-stranded DNA by active transcription through the binding site. These results provide a potential mechanism by which TIAR can shuttle between RNA and DNA ligands.

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Heterogeneous nuclear ribonucleoprotein D0B is a sequence-specificDNA-binding protein

Cited by 38 publications

References 34 publications

Viral DNA Replication Orientation and hnRNPs Regulate Transcription of the Human Papillomavirus 18 Late Promoter

Viral DNA Replication Orientation and hnRNPs Regulate Transcription of the Human Papillomavirus 18 Late Promoter

Kruppel-like factor 2 Transcriptional Regulation Involves Heterogeneous Nuclear Ribonucleoproteins and Acetyltransferases

Novel DNA-binding properties of the RNA-binding protein TIAR

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