Cloning and Characterization of Rat Cellular Nucleic Acid Binding Protein (CNBP) cDNA

Yasuda, Jun; Mashiyama, Shoji; Makino, Reiko; Ohyama, Shigekazu; Sekiya, Takao; Hayashi, Kenshi

doi:10.1093/dnares/2.1.45

Cited by 35 publications

(30 citation statements)

References 20 publications

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“…[31][32][33][34][35] This is consistent with our findings in normal controls, where overall ZNF9 expression is higher in slow type 1 fibers than in fast type 2 fibers and early differentiating myocytes (data not shown). However, the localization of ZNF9 changing from the nuclei in undifferentiated myoblasts to the cytoplasm during differentiation to myotubes and the cytoplasmic localization of ZNF9 in mature human muscle fibers in sarcomeric striations at the Z-disks 36 is unexpected for a transcription factor and suggestive of other functions in mature muscle fibers.…”

Section: Discussionsupporting

confidence: 91%

Mutant (CCTG)n Expansion Causes Abnormal Expression of Zinc Finger Protein 9 (ZNF9) in Myotonic Dystrophy Type 2

Raheem

Olufemi

Bachinski

et al. 2010

The American Journal of Pathology

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The mutation that underlies myotonic dystrophy type 2 (DM2) is a (CCTG)n expansion in intron 1 of zinc finger protein 9 (ZNF9). It has been suggested that ZNF9 is of no consequence for disease pathogenesis. We determined the expression levels of ZNF9 during muscle cell differentiation and in DM2 muscle by microarray profiling, real-time RT-PCR, splice variant analysis, immunofluorescence, and Western blotting. Our results show that in differentiating myoblasts, ZNF9 protein was localized primarily to the nucleus, whereas in mature muscle fibers, it was cytoplasmic and organized in sarcomeric striations at the Z-disk. In patients with DM2 , ZNF9 was abnormally expressed. First, there was an overall reduction in both the mRNA and protein levels. Second, the subcellular localization of the ZNF9 protein was somewhat less cytoplasmic and more membrane-bound. Third, our splice variant analysis revealed retention of intron 3 in an aberrant isoform, and fourth quantitative allelespecific expression analysis showed the persistence of intron 1 sequences from the abnormal allele, further suggesting that the mutant allele is incompletely spliced. Thus, the decrease in total expression appears to be due to impaired splicing of the mutant transcript. Our data indicate that ZNF9 expression in DM2 patients is altered at multiple levels. Although toxic RNA effects likely explain overlapping phenotypic manifestations between DM1 and DM2, abnormal ZNF9 levels in DM2 may account for the differences in DM1.

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Section: Discussionsupporting

confidence: 91%

Mutant (CCTG)n Expansion Causes Abnormal Expression of Zinc Finger Protein 9 (ZNF9) in Myotonic Dystrophy Type 2

Raheem

Olufemi

Bachinski

et al. 2010

The American Journal of Pathology

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“…It contains seven tandem zinc finger repeats that are composed of 14 same amino acid arrangement of Cys-X2 -Cys -X4 -His-X4 -Cys (Armas et al, 2001). So far, CNBP cDNAs have been cloned from human (Rajavashisth et al, 1989), mouse (Warden et al, 1994), rat (Yasuda et al, 1995), chicken (Van Heumen et al, 1997), Xenopus (Flink et al, 1998), Bufo arenarum (Armas et al, 2001), and Danio rerio (Armas et al, 2004), and all of them have been demonstrated to be highly conserved at the amino acid and nucleotide levels.…”

Section: Introductionmentioning

confidence: 99%

Expression pattern and developmental behaviour of cellular nucleic acid-binding protein (CNBP) during folliculogenesis and oogenesis in fish

Liu

Gui

2005

Gene

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“…Cellular nucleic acid binding protein (CNBP), also known as zinc-finger protein 9 (ZNF9), is a zinc-finger protein that binds single-stranded DNA (ssDNA) [Rajavashisth et al, 1989;Michelotti et al, 1995] and RNA [Yasuda et al, 1995;Pellizzoni et al, 1997;Calcaterra et al, 1999;Armas et al, 2004] molecules. CNBP cDNAs have been cloned from mammals [Michelotti et al, 1995;Yasuda et al, 1995;Flink and Morkin, 1995b;Shimizu et al, 2003], chicken [Ruble and Foster, 1998], fish [Armas et al, 2004;Liu and Gui, 2005], and amphibians [Pellizzoni et al, 1997;Armas et al, 2001].…”

mentioning

confidence: 99%

Cellular nucleic acid binding protein binds G‐rich single‐stranded nucleic acids and may function as a nucleic acid chaperone

Armas

Nasif

Calcaterra

2007

J of Cellular Biochemistry

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Cellular nucleic acid binding protein (CNBP) is a small single-stranded nucleic acid binding protein made of seven Zn knuckles and an Arg-Gly rich box. CNBP is strikingly conserved among vertebrates and was reported to play broad-spectrum functions in eukaryotic cells biology. Neither its biological function nor its mechanisms of action were elucidated yet. The main goal of this work was to gain further insights into the CNBP biochemical and molecular features. We studied Bufo arenarum CNBP (bCNBP) binding to single-stranded nucleic acid probes representing the main reported CNBP putative targets. We report that, although bCNBP is able to bind RNA and single-stranded DNA (ssDNA) probes in vitro, it binds RNA as a preformed dimer whereas both monomer and dimer are able to bind to ssDNA. A systematic analysis of variant probes shows that the preferred bCNBP targets contain unpaired guanosine-rich stretches. These data expand the knowledge about CNBP binding stoichiometry and begins to dissect the main features of CNBP nucleic acid targets. Besides, we show that bCNBP presents a highly disordered predicted structure and promotes the annealing and melting of nucleic acids in vitro. These features are typical of proteins that function as nucleic acid chaperones. Based on these data, we propose that CNBP may function as a nucleic acid chaperone through binding, remodeling, and stabilizing nucleic acids secondary structures. This novel CNBP biochemical activity broadens the field of study about its biological function and may be the basis to understand the diverse ways in which CNBP controls gene expression.

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Cloning and Characterization of Rat Cellular Nucleic Acid Binding Protein (CNBP) cDNA

Cited by 35 publications

References 20 publications

Mutant (CCTG)n Expansion Causes Abnormal Expression of Zinc Finger Protein 9 (ZNF9) in Myotonic Dystrophy Type 2

Mutant (CCTG)n Expansion Causes Abnormal Expression of Zinc Finger Protein 9 (ZNF9) in Myotonic Dystrophy Type 2

Expression pattern and developmental behaviour of cellular nucleic acid-binding protein (CNBP) during folliculogenesis and oogenesis in fish

Cellular nucleic acid binding protein binds G‐rich single‐stranded nucleic acids and may function as a nucleic acid chaperone

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