Binding of a bZip protein to the estrogen-inducible apoVLDL II promoter

Smidt, Marten P.; Wijnholds, Jan; Snippe, Lenie; Keulen, Geertje van; Ab, Geert

doi:10.1016/0167-4781(94)90253-4

Cited by 7 publications

(17 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The hnRNP D0 Proteins as Members of the 2xRBD-Gly Family-A homology search of GenBank TM (release 87) indicated that many RNA-binding proteins have significant homology with the hnRNP D0 proteins: the DNA binding protein E2BP (14), the hnRNP C type protein (12), the AϩU-rich RNA binding protein AUF1 (17,18), the hnRNP type A/B protein (19), the CArG box binding protein (20), the D-box binding protein (21), the hrp40 proteins produced by Drosophila squid gene (22,23), the hnRNP A1 protein, the hnRNP A2/B1 proteins, and the Xenopus hnRNP A2 family proteins. Among them, E2BP, the hnRNP C type protein, and AUF1 show an almost identical amino acid sequence with the hnRNP D0 proteins and thus are most likely derived from the same gene.…”

Section: Hnrnp D0 a 2xrbd-gly Type Of Rna-binding Proteinmentioning

confidence: 99%

The UUAG-specific RNA Binding Protein, Heterogeneous Nuclear Ribonucleoprotein D0

Kajita

Nakayama²,

Aizawa

et al. 1995

Journal of Biological Chemistry

103

View full text Add to dashboard Cite

Human cDNA clones encoding the UUAG-binding heterogeneous nuclear ribonucleoprotein (hnRNP) D0 protein have been isolated and expressed. The protein has two RNA-binding domains (RBDs) in the middle part of the protein and an RGG box, a region rich in glycine and arginine residues, in the C-terminal part ("2xRBD-Gly" structure). The hnRNP A1, A2/B1, and D0 proteins, all possess common features of the 2xRBD-Gly structure and binding specificity toward RNA. Together, they form a subfamily of RBD class RNA binding proteins (the 2xRBD-Gly family). One of the structural characteristics shared by these proteins is the presence of several isoforms presumably resulting from alternative splicing. Filter binding assays, using the recombinant hnRNP D0 proteins that have one of the two RBDs, indicated that one RBD specifically binds to the UUAG sequence. However, two isoforms with or without a 19-amino acid insertion at the N-terminal RBD showed different preference toward mutant RNA substrates. The 19-amino acid insertion is located in the N-terminal end of the first RBD. This result establishes the participation of the N terminus of RBD in determining the sequence specificity of binding. A similar insertion was also reported with the hnRNP A2/B1 proteins. Thus, it might be possible that this type of insertion with the 2xRBD-Gly type RNA binding proteins plays a role in "fine tuning" the specificity of RNA binding. RBD is supposed to bind with RNA in general and sequencespecific manners. These two discernible binding modes are proposed to be performed by different regions of the RBD. A structural model of these two binding sites is presented.Ribonucleoproteins have been found in many macromolecular complexes that have vital biological roles, such as heterogeneous nuclear ribonucleoprotein (hnRNP) 1 (1), small nuclear ribonucleoprotein (snRNP), ribosomes, and signal recognition particles. These complexes are composed of RNAs and proteins, many of which show RNA binding activities. One of the most common groups of RNA binding proteins is the RBD class proteins (2). They possess a CS-RBD (consensus sequence-RNA binding domain) motif, which is typically 80 -90 amino acids. Two short sequences, RNP 2 octamer and RNP 1 hexamer, have been found to be conserved among different RBDs. Several RBDs are commonly found in tandem within one molecule. It is also common to find an auxiliary RNA-binding motif present in addition to RBDs within the same molecule. Thus, RBD class RNA binding proteins typically possess several RNA-binding domains as modules. It has not been well studied, however, how these modular domains participate together in binding with RNA. hnRNP proteins are a subset of proteinaceous components found in hnRNP, which is a large complex formed by the nascent pre-mRNA and proteins (1, 3). More than 20 proteins have been identified as hnRNP proteins on two-dimensional protein gel electrophoresis. Although structures of all of these proteins are not known, many contain RBDs, which are the regions responsible for interaction ...

show abstract

Section: Hnrnp D0 a 2xrbd-gly Type Of Rna-binding Proteinmentioning

confidence: 99%

The UUAG-specific RNA Binding Protein, Heterogeneous Nuclear Ribonucleoprotein D0

Kajita

Nakayama²,

Aizawa

et al. 1995

Journal of Biological Chemistry

103

View full text Add to dashboard Cite

show abstract

“…Also, overlap with CCAAT/enhancer-binding sites (C/EBP) has been reported [15,16]. The elements D, F and B2 of the verylow-density apolipoprotein II (apoVLDL II) 5′-flanking region are high-affinity binding sites for VBP [3], as expected on the basis of their similarity to the albumin site D sequence. The apoVLDL II site D is of special interest because of its proximity to the major estrogen-responsive element (ERE), spanning positions Ϫ157 to Ϫ176 [17].…”

mentioning

confidence: 87%

“…This delay suggests a role for DBP in HLF expression [9]. Reflecting their very similar DNA-binding domains, all the PAR proteins recognise identical or almost identical DNA-bindings sites [1,3,7,8,10]. Also, overlap with CCAAT/enhancer-binding sites (C/EBP) has been reported [15,16].…”

mentioning

confidence: 99%

mentioning

confidence: 99%

“…In addition to these four isoforms, a longer mRNA, resulting from an alternative polyadenylation site located in exon 5, was identified [2]. The described AA form represents the liver transcript [1,3].The albumin-site-D-binding protein (DBP) [7], the hepatic leukaemia factor (HLF) [8,9], the thyrotroph embryonic factor (TEF) [10] and Drosophila par domain protein 1 (PDP1) [11] Correspondence to M. P. Smidt, Department of Medical Pharmacology, Rudolf Magnus Institute for Neurosciences, Universiteitsweg 100, NL-3584 CG Utrecht, The Netherlands Fax: ϩ31 30 2539032. E-mail: Smidt@med.ruu.nl Abbreviations.…”

mentioning

confidence: 99%

See 2 more Smart Citations

The bZip transcription factor vitellogenin‐binding protein is post transcriptional down regulated in chicken liver

Smidt

Snippe

Keulen

et al. 1998

European Journal of Biochemistry

Self Cite

View full text Add to dashboard Cite

The vitellogenin-binding protein (VBP) is a member of the proline and acidic-region rich (PAR) family of bZip transcription factors. PAR is located N-terminally to the DNA-binding domain. VBP binds to specific sites within the 300-bp 5′-flanking region of the chicken-liver-specific estrogen-dependent very-low-density apolipoprotein gene (apoVLDL II). One of these binding sites (site D) resembles the albumin site D and is positioned in close proximity of the major estrogen-responsive element. Previous studies showed that VBP can bind simultaneously with the estrogen receptor to the putative complex regulatory element E1D. To investigate whether VBP is involved in apoVLDL II gene expression, we examined its capacity to enhance apoVLDL II transcription and its presence in liver. We show that VBP is capable of enhancing transcription in transfection experiments. However, VBP could not be detected in liver by Western-blots or immuno-electro mobility shift assays (EMSAs) using antibodies against different moieties of the protein. We examined the possible reduction in translation efficienies due to a small upstream open reading frame in the VBP leader sequence, but did not find any. Although VBP binds to the proximal apoVLDL II promoter region and enhances transcription in co-transfection experiments, the protein is unlikely to be involved in apoVLDL II gene transcription because of its undetectable low level in liver nuclei. . The VBP gene consist of six exons, which can form four different mRNAs by alternative usage of exons 1 and 2 for the N-terminus and exons 5 and 6 for the C-terminus [2]. The corresponding protein isoforms are called AA, βA, Aβ and ββ, depending whether they are encoded by exon 1-3-4-5, 1-3-4-6, 2-3-4-5 or 2-3-4-6, respectively. In addition to these four isoforms, a longer mRNA, resulting from an alternative polyadenylation site located in exon 5, was identified [2]. The described AA form represents the liver transcript [1,3].The albumin-site-D-binding protein (DBP) [7], the hepatic leukaemia factor (HLF) [8,9], the thyrotroph embryonic factor (TEF) [10] and Drosophila par domain protein 1 (PDP1) [11] Correspondence to M. P. Smidt, Department of Medical Pharmacology, Rudolf Magnus Institute for Neurosciences, Universiteitsweg 100, NL-3584 CG Utrecht, The Netherlands Fax: ϩ31 30 2539032. E-mail: Smidt@med.ruu.nl Abbreviations. VBP, vitellogenine binding protein ; ApoVLDL II, very-low-density apolipoprotein II; PAR, proline and acidic-region rich; ERE, estrogen-responsive element; EMSA, electromobility assay ; uORF, upstream open reading frame; DBP, albumin-site-D-binding protein; HLF, hepatic nuclear factor; TEF, thyrotroph embryonic factor; PDP1, par domain protein 1; C/CEBP, CCAAT-enhancer-binding protein; TK-CAT, timidine kinase-chloramphenicol acetyl tranferase; LMH, leghorn strain M ; HRP, horse radish peroxidase ; ssDBF, single-stand-DNA-binding factor; CPA1, carbamoyl-phosphate synthase A; CMV, cytomegalovirus.are other members of the PAR subfamily. TEF was cloned from rat brain and, on the...

show abstract

A Composite Regulatory Element in the First Intron of the Estrogen-Responsive Very Low Density Apolipoprotein II Gene

Shuler¹,

Chu²,

Wang³

et al. 1998

DNA and Cell Biology

View full text Add to dashboard Cite

Binding of a bZip protein to the estrogen-inducible apoVLDL II promoter

Cited by 7 publications

References 27 publications

The UUAG-specific RNA Binding Protein, Heterogeneous Nuclear Ribonucleoprotein D0

The UUAG-specific RNA Binding Protein, Heterogeneous Nuclear Ribonucleoprotein D0

The bZip transcription factor vitellogenin‐binding protein is post transcriptional down regulated in chicken liver

A Composite Regulatory Element in the First Intron of the Estrogen-Responsive Very Low Density Apolipoprotein II Gene

Contact Info

Product

Resources

About