cDNA cloning and developmental expression of cellular nucleic acid-binding protein (CNBP) gene in Xenopus laevis

Dominicis, A. De; Lotti, Francesco; Pierandrei-Amaldi, Paola; Cardinali, Beatrice

doi:10.1016/s0378-1119(99)00471-0

Cited by 21 publications

(28 citation statements)

References 27 publications

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“…The amino acid sequence of CNBP is highly conserved; the sequence of human CNBP is 94.1% identical to that of Xenopus (Flink et al, 1998). De Dominicis et al further reported that, in Xenopus embryos, CNBP mRNA accumulation during development decreases before the mid-blastula stage and increases again thereafter (De Dominicis et al, 2000). Although the in vivo role and expression pattern of CNBP in mammalian development remains unclear, the extraordinary level of conservation and the expression pattern in Xenopus embryos suggest a potentially important role for CNBP during early embryonic development across different species.…”

Section: Introductionmentioning

confidence: 99%

The zinc-finger protein CNBP is required for forebrain formation in the mouse

Chen

Liang²,

Deng³

et al. 2003

Development

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Mouse mutants have allowed us to gain significant insight into axis development. However, much remains to be learned about the cellular and molecular basis of early forebrain patterning. We describe a lethal mutation mouse strain generated using promoter-trap mutagenesis. The mutants exhibit severe forebrain truncation in homozygous mouse embryos and various craniofacial defects in heterozygotes. We show that the defects are caused by disruption of the gene encoding cellular nucleic acid binding protein (CNBP);Cnbp transgenic mice were able to rescue fully the mutant phenotype.Cnbp is first expressed in the anterior visceral endoderm (AVE) and,subsequently, in the anterior definitive endoderm (ADE), anterior neuroectoderm (ANE), anterior mesendoderm (AME), headfolds and forebrain. InCnbp-/- embryos, the visceral endoderm remains in the distal tip of the conceptus and the ADE fails to form, whereas the node and notochord form normally. A substantial reduction in cell proliferation was observed in the anterior regions of Cnbp-/- embryos at gastrulation and neural-fold stages. In these regions, Myc expression was absent, indicating CNBP targets Myc in rostral head formation. Our findings demonstrate that Cnbp is essential for the forebrain induction and specification.

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Section: Introductionmentioning

confidence: 99%

The zinc-finger protein CNBP is required for forebrain formation in the mouse

Chen

Liang²,

Deng³

et al. 2003

Development

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“…The predominant localization of CNBP in the cytoplasm or the endoplasmic reticulum is consistent with its preferential binding to specific RNA sequences (Warden et al, 1994). Recently, Pierandrei-Amaldi and co-workers have identified CNBP in vitro as a key translation regulator of TOP-containing ribosomal protein-encoding mRNAs in Xenopus (De Dominicis et al, 2000).…”

Section: Introductionmentioning

confidence: 61%

Novel CNBP‐ and La‐based translation control systems for mammalian cells

Schlatter

Fussenegger²

2002

Biotech & Bioengineering

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Throughout the development of Xenopus, production of ribosomal proteins (rp) is regulated at the translational level. Translation control is mediated by a terminal oligopyrimidine element (TOP) present in the 5Ј untranslated region (UTR) of rp-encoding mRNAs. TOP elements adopt a specific secondary structure that prevents ribosome-binding and translation-initiation of rpencoding mRNAs. However, binding of CNBP (cellular nucleic acid binding protein) or La proteins to the TOP hairpin structure abolishes the TOP-mediated transcription block and induces rp production. Based on the specific CNBP-TOP/La-TOP interactions we have designed a translation control system (TCS) for conditional as well as adjustable translation of desired transgene mRNAs in mammalian cells. The generic TCS configuration consists of a plasmid encoding CNBP or La under control of the tetracycline-responsive expression system (TET OFF ) and a target expression vector containing a TOP module between a constitutive P SV40 promoter and the human model product gene SEAP (human secreted alkaline phosphatase) (P SV40 -TOP-SEAP-pA). The TCS technology showed excellent SEAP regulation profiles in transgenic Chinese hamster ovary (CHO) cells. Alternatively to CNBP and La, TOP-mediated translation control can also be adjusted by artificial phosphorothioate anti-TOP oligodeoxynucleotides. Confocal laser-scanning microscopy demonstrated cellular uptake of FITC-labeled oligodeoxynucleotides and their localization in perinuclear organelles within 24 hours. Besides their TOP-based translation-controlling capacity, CNBP and La were also shown to increase cap-independent translation from polioviral internal ribosomal entry sites (IRES) and La alone to boost cap-dependent translation initiation. CNBP and La exemplify for the first time the potential of RNAbinding proteins to exert translation control of desired transgenes and to increase heterologous protein production in mammalian cells. We expect both of these assets to advance current gene therapy and biopharmaceutical manufacturing strategies.

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“…Surprisingly, there is a class of proteins called cellular nucleic acid binding proteins (CNBPs) that contain seven Zn 2ϩ finger sequences that are very similar to those found in retroviral NC (3,6,12,35,45,47,55). Retroviral NC and CNBP Zn 2ϩ fingers have arrangements of amino acids with the general sequence: "-Cys--X-Cys-Gly-Ϯ-X-Gly-His-X 3 -␦-Cys-," where X is a variable amino acid, is an aromatic residue, "Ϯ" is a charged amino acid, and ␦ is a carbonylcontaining residue.…”

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confidence: 99%

“…CNBPs from a number of vertebrates are highly homologous at the protein and nucleic acid levels. They have been found in humans (45), rodents (6,35,55), chickens (47), and amphibians (3,12).…”

mentioning

confidence: 99%