A general transcription factor forms a stable complex with RNA polymerase B (II)

Zheng, Xiujun; Moncollin, Vincent; Egly, Jean‐Marc; Chambon, Pierre

doi:10.1016/0092-8674(87)90490-9

Cited by 173 publications

(112 citation statements)

References 30 publications

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“…Similarly, isolated βNAC (also called BTF3b) was initially identified as an alternative splicing isoform of the basic transcription factor (BTF3a). However, βNAC is transcriptionally inactive although it has the same ability as BTF3a to bind RNA polymerase II (Zheng et al, 1987(Zheng et al, , 1990. Structural basis of such distinct functions remains to be determined.…”

Section: Introductionmentioning

confidence: 99%

Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its αNAC subunit

et al. 2010

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Nascent polypeptide associated complex (NAC) and its two isolated subunits, αNAC and βNAC, play important roles in nascent peptide targeting. We determined a 1.9 Å resolution crystal structure of the interaction core of NAC heterodimer and a 2.4 Å resolution crystal structure of αNAC NAC domain homodimer. These structures provide detailed information of NAC heterodimerization and αNAC homodimerization. We found that the NAC domains of αNAC and βNAC share very similar folding despite of their relative low identity of amino acid sequences. Furthermore, different electric charge distributions of the two subunits at the NAC interface provide an explanation to the observation that the heterodimer of NAC complex is more stable than the single subunit homodimer. In addition, we successfully built a βNAC NAC domain homodimer model based on homologous modeling, suggesting that NAC domain dimerization is a general property of the NAC family. These 3D structures allow further studies on structurefunction relationship of NAC.

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Section: Introductionmentioning

confidence: 99%

Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its αNAC subunit

et al. 2010

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“…13 We have previously identified BTF3 as a differentially expressed gene in PDAC and chronic pancreatitis (CP). 14,15 In the present study we: (1) analyzed the expression of BTF3 mRNA and protein in the normal and diseased pancreas (CP and PDAC) and pancreatic cancer cell lines, and the localization of BTF3 in these tissues; (2) analyzed the functional consequences of BTF3 silencing in pancreatic cancer cell lines in terms of resistance to chemo/radiotherapy-induced apoptosis, and (3) used a DNA micro-array analysis to identify regulation of genes after BTF3 silencing, in order to specify the role of BTF3 in the transcriptional regulation of tumor-associated genes.…”

Section: Introductionmentioning

confidence: 99%

“…1,3,4 BTF3 is present in two isoforms: BTF3a, which has the transcription characteristics of BTF3, and BTF3b, which lacks the first 44 amino acids of BTF3a and is transcriptionally inactive. 4,5 BTF3 is also able to inhibit the transcription of genes such as GAL, which acts as a paracrine regulator of prolactin expression.…”

Section: Introductionmentioning

confidence: 99%

“…Basic transcription factor 3 (BTF3), also known as nascent polypeptide-associated complex b (NACB), is a 27 KD protein 1,2 that is involved in the initiation of transcription by RNA polymerase from proximal promoter elements such as the TATA box and CAAT box sequences. 1,3,4 BTF3 is present in two isoforms: BTF3a, which has the transcription characteristics of BTF3, and BTF3b, which lacks the first 44 amino acids of BTF3a and is transcriptionally inactive.…”

Section: Introductionmentioning

confidence: 99%

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Basic transcription factor 3 (BTF3) regulates transcription of tumor-associated genes in pancreatic cancer cells

Kusumawidjaja

Kayed

Giese

et al. 2007

Cancer Biology & Therapy

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Basic transcription factor 3 (BTF3) acts as a transcription factor and modulator of apoptosis, and is differentially expressed in colorectal cancer and glioblastomas. In the present study, the expression of BTF3, as well as its role in apoptosis and gene transcription, was analyzed in pancreatic ductal adenocarcinoma (PDAC). QRT-PCR, immunohistochemistry, immunoblotting, and immunofluorescence analyses were carried out to investigate BTF3 mRNA/protein expression and localization. BTF3 silencing in pancreatic cancer cells was performed using specific siRNA molecules. Functional analyses were carried out using cell growth assays, apoptosis assays, and DNA array analysis. BTF3 and BTF3a exhibited 1.3-fold and 4.6-fold increased median mRNA levels in PDAC tissues, compared to normal pancreatic tissues. BTF3 localized mainly in the cytoplasm and nuclei of tubular complexes and pancreatic cancer cells. Pancreatic cancer cell lines expressed the mRNA and protein of BTF3a (27 kDa) and BTF3b (22 kDa) isoforms. BTF3 silencing using specific siRNA molecules did not influence apoptosis induced by chemotherapy or radiotherapy. In contrast, BTF3 silencing resulted in down-regulation of several cancer-associated genes, including EPHB2, ABL2, HPSE2 and ATM, and up-regulation of KRAG, RRAS2, NFk-B, MRVI1, MADCAM1 and others. In conclusion, BTF3 is overexpressed in PDAC, where it acts as a transcriptional regulator rather than a direct modulator of apoptosis.

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“…It is evolutionary conserved and presents in a variety of mammalian cells [1,2]. Its biological importance is shown by the fact that an insertional mutation in the BTF3 leads to an early postimplantation lethality in mice [3].…”

Section: Introductionmentioning

confidence: 99%

Clinicopathological significance of BTF3 expression in colorectal cancer

et al. 2013

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Basic transcription factor 3 (BTF3) is a general RNA polymerase II transcription factor, and also involved in apoptosis regulation. Increasing evidence shows that BTF3 is aberrantly expressed in several kinds of malignancies, but there is no study to analyze BTF3 expression in colorectal cancer (CRC) patients. Applying immunohistochemistry, we detected BTF3 in CRCs (n = 156), the corresponding distant (n = 42), adjacent normal mucosa (n = 96), lymph node metastases (n = 35), and analyzed its relationships with clinicopatholocial and biological variables. Our results showed that BTF3 staining significantly increased from distant or adjacent normal mucosa to primary CRCs (p<0.0001) or metastases (p=0.002 and p<0.0001). BTF3 was higher in distal cancers than in proximal cancers (57% vs. 39%, p=0.041).It also showed stronger staining in primary CRCs stage I and II than that in stage III and IV (64% vs. 35%, p=0.0004), or metastases (64% vs. 29%, p=0.004). Cancers with better differentiation had a higher expression than those with worse differentiation (56% vs. 37%, p=0.031). There were positive correlations of BTF3 expression with NF-κB, RAD50, MRE11, NBS1 and AEG-1 (p<0.05). In conclusion, BTF3 overexpression may be an early event in CRC development, and could be useful biomarker for the early stage of CRCs. BTF3 has positive correlations with NF-κB, RAD50, MRE11, NBS1 and AEG-1, and might influence complex signal pathways in CRC. Wang CJ et al. 4

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A general transcription factor forms a stable complex with RNA polymerase B (II)

Cited by 173 publications

References 30 publications

Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its αNAC subunit

Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its αNAC subunit

Basic transcription factor 3 (BTF3) regulates transcription of tumor-associated genes in pancreatic cancer cells

Clinicopathological significance of BTF3 expression in colorectal cancer

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