Mammalian heterogeneous nuclear ribonucleoprotein complex protein A1. Large-scale overproduction in Escherichia coli and cooperative binding to single-stranded nucleic acids.

Cobianchi, Fabio; Karpel, Richard L.; Williams, Kenneth R.; Notario, Vincente; Wilson, Samuel H.

doi:10.1016/s0021-9258(19)35461-4

Cited by 161 publications

(35 citation statements)

References 42 publications

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“…This yeast DNA sequence directed expression of a 67 kDa polypeptide that remained insoluble under the extraction conditions used. The identity of the protein was confirmed by NH2-terminal amino acid sequencing; the NH2-terminal methionine was absent, by virtue of an unknown mechanism, as was observed earlier for intact ,B-pol, 8 kDa domain of ,B-pol, hnRNPA1, and HIV-1 RT expressed proteins in E. coli (22)(23)(24)(25).…”

Section: Discussionsupporting

confidence: 53%

Yeast open reading frame YCR14C encodes a DNA β-polymerase-like enzyme

Prasad¹,

Widen²,

Singhal³

et al. 1993

Nucl Acids Res

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We have shown by activity gel that overexpression in E. coli of a yeast chromosome 3 open reading frame (ORF) designated YCR14C and bearing homology to mammalian DNA polymerases beta results in a new DNA polymerase in the host cells. The molecular mass of this enzyme corresponded to the YCR14C-predicted 67 kDa protein, and NH2-terminal amino acid sequencing confirmed that the expressed protein was encoded by the yeast ORF. This new yeast DNA polymerase was purified to homogeneity from E.coli. In a fashion similar to that of mammalian beta-polymerases, the purified yeast enzyme exhibited distributive DNA synthesis on DNA substrate with a single-stranded template and processive gap-filling synthesis on a short-gapped DNA substrate. Activity of this yeast beta-polymerase-like enzyme was sensitive to the beta-polymerase inhibitor ddNTP and resistant to both 1 mM NEM and neutralizing antibody to E. coli DNA polymerase I. These results, therefore, indicate that YCR14C encodes a DNA beta-polymerase-like enzyme in yeast, and we name it DNA polymerase IV. Yeast strains harboring a deletion mutation of the pol IV gene are viable, they exhibit no increase in sensitivity to ultraviolet light, ionizing radiation or alkylating agents, and sporulation and spore viability are not affected in the mutant.

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Section: Discussionsupporting

confidence: 53%

Yeast open reading frame YCR14C encodes a DNA β-polymerase-like enzyme

Prasad¹,

Widen²,

Singhal³

et al. 1993

Nucl Acids Res

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“…A carboxyl-terminal glycine-rich domain is a common feature of many of the major hnRNP proteins . The glycinerich domain of the mammalian ImRNP Al has been reported to bind directly to single-stranded nucleic acids (Cobianchi et al ., 1988 ; and to have RNA-RNA strand annealing-promoting activity . Therefore, a possible explanation for the variation seen in the glycine-rich domains of the hrp proteins is that these differences confer specialized RNA-binding capabilities.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the major hnRNP proteins from Drosophila melanogaster.

Matunis

Dreyfuss

1992

The Journal of Cell Biology

125

107

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. To better understand the role(s) of hnRNP proteins in the process of mRNA formation, we have identified and characterized the major nuclear proteins that interact with hnRNAs in Drosophila melanogaster. cDNA clones of several D. melanogaster hnRNP proteins have been isolated and sequenced, and the genes encoding these proteins have been mapped cytologically on polytene chromosomes . These include the hnRNP proteins hrp36, hrp40, and hrp48, which together account for the major proteins of hnRNP complexes in D. melanogaster (Matunis et al., 1992, accompanying paper) . All of the proteins described here contain two amino-terminal RNP consensus sequence RNA-binding domains and a carboxyl-terminal glycine-rich domain . We refer to this configuration, which is also found in the hnRNP A/B proteins of vertebrates, as 2XRBD-Gly. The sequences of the H ETEROGENEous nuclear RNAs (hnRNAs), from which mRNAs in eukaryotic cells are derived by RNA processing, are associated with specific nuclear proteins and form heterogeneous nuclear RNP (hnRNP)

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“…In the next set of experiments, VSMCs were pretreated with the RGG peptide. The RGG motif was initially described as an RNA-binding motif in several proteins [29][30][31]. The RGG domain of nucleolin was recently demonstrated to be involved in protein-protein interaction [32].…”

Section: Ck2 and Nucleolin Are Involved In The Upa-induced Cell Proliferationmentioning

confidence: 99%