Cloning and sequencing of the human nucleolin cDNA

Srivastava, Meera; Fleming, Patrick; Pollard, Harvey B.; Burns, A. Lee

doi:10.1016/0014-5793(89)80692-1

Cited by 130 publications

(90 citation statements)

References 36 publications

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“…A preferred affinity for single-stranded nucleic acids has also been found for the RGG domains from hnRNP A1 (13), hnRNP U (14), and nucleolin (15). The RGG-box of nucleolin displays a ␤-spiral structure that binds single-stranded nucleic acids with an induced base unstacking effect (39), most likely with the consequence of duplex unwinding (40).…”

Section: Discussionmentioning

confidence: 96%

“…The carboxylterminal 100 amino acids of NDH II consist of a consecutive stretch of glycines that is regularly interrupted by either aromatic amino acids or arginine. Similar RGG-rich sequences (RGG-boxes) have been found as part of many nucleic acidbinding proteins, such as the heterogeneous nuclear ribonucleoproteins hnRNP A1 (13) and hnRNP U (14), nucleolin (15), yeast single-strand DNA-binding protein 1 (16), as well as of other proteins from the superfamily of DEX(D/H) helicases (17)(18)(19)(20)(21)(22)(23). Except hnRNP U, where the RGG-box is the only nucleic acid binding domain (14), RGG-boxes cooperate with other domains to achieve an increased affinity for nucleic acids.…”

mentioning

confidence: 99%

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Domain Structure of Human Nuclear DNA Helicase II (RNA Helicase A)

Zhang¹,

Grosse²

1997

Journal of Biological Chemistry

108

125

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Full-length human nuclear DNA helicase II (NDH II) was cloned and overexpressed in a baculovirus-derived expression system. Recombinant NDH II unwound both DNA and RNA. Limited tryptic digestion produced active helicases with molecular masses of 130 and 100 kDa. The 130-kDa helicase missed a glycine-rich domain (RGG-box) at the carboxyl terminus, while the 100-kDa form missed both its double-stranded RNA binding domains (dsRBDs) at the amino terminus and its RGG-box. Hence, the dsRBDs and the RGG-box were dispensable for unwinding. On the other hand, the isolated DEXH core alone could neither hydrolyze ATP nor unwind nucleic acids. These enzymatic activities were not regained by fusing a complete COOH or NH 2 terminus to the helicase core. Hence, an active helicase required part of the NH 2 terminus, the DEXH core, and a C-terminal extension of the core. Both dsRBDs and the RGGbox were bacterially expressed as glutathione S-transferase fusion proteins. The two dsRBDs had a strong affinity to double-stranded RNA and cooperated upon RNA binding, while the RGG-box bound preferentially to single-stranded DNA. A model is suggested in which the flanking domains influence and regulate the unwinding properties of NDH II.Nuclear DNA helicase II (NDH II) 1 was originally isolated from calf thymus by assaying its DNA unwinding activity (1). Subsequently, it was shown that NDH II also contains RNA helicase activity (2). The cDNA sequence of NDH II (3) revealed a high homology to two previously known proteins, namely human RNA helicase A (4) and the Drosophila "maleless" protein (MLE) (5). From the cDNA sequences it was also deduced that the three proteins belong to the superfamily of DEXH helicases, all members of which possess seven conserved helicase motifs in the putative catalytically active core. The presence of the DEXH helicase core domain suggests a function in RNA and/or DNA unwinding for all three members of this superfamily. The core contains an ATP binding site with the consensus sequence GCGKT (A site) and FILDD (B site) in motif

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Section: Discussionmentioning

confidence: 96%

mentioning

confidence: 99%

Domain Structure of Human Nuclear DNA Helicase II (RNA Helicase A)

Zhang¹,

Grosse²

1997

Journal of Biological Chemistry

108

125

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“…hnRNP, heterogenous nuclear ribonucleoprotein ; KH domain, a peptide motif identified originally in hnRNP-K; PCBP, poly(C)-binding protein; CS-RBD, consensus-sequence RNA-binding domain; RRM, RNA recognition motif; 2D, two-dimensional. fuss et al, 1993) and this motif was also found in RRM-motifcontaining proteins, including nucleolin (Srivastava et al, 1989). This motif consists of one or more RGG boxes, that are repetitions of an Arg-Gly-Gly sequence interspersed with other, often aromatic, amino acids and it has been shown to interact directly with RNA (Kiledijan and Dreyfuss, 1992;Ghisolfi et al, 1992).…”

Section: Hagen Denmarkmentioning

confidence: 96%

Characterisation of the Nucleic‐Acid‐Binding Activity of KH Domains Different Properties of Different Domains

Dejgaard

Leffers

1996

European Journal of Biochemistry

116

114

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The KH module is a sequence motif recently identified in a number of diversified RNA-binding proteins and suggested to be the functional element responsible for RNA binding. So far, however, this hypothesis has not received direct experimental support. We have expressed the three KH-domains from heterogeneous nuclear ribonucleoprotein K (hnRNP-K), the poly(C)-binding proteins PCBP-1 and PCBP-2, the first three to four domains from the high-density binding protein HBP, the one and a half domain from the archaeon Halobacterium halobium ORF139 and one and a half domain of the fragile-X protein FMRl in Escherichia coli and analysed their nucleic-acid-binding properties in vitro. The results showed that the in vitro poly(rC)-binding activity of hnRNP-K can be assigned to KH-domain 3, whereas both domains 1 and 3 in the PCBPs bind poly(rC). In addition, all these domains exhibit binding activity towards other nucleic acids, albeit at a significantly lower level. The first KH domain from the FMRl protein binds poly(rG) and single-stranded and double-stranded DNA. The N-terminal three or four domains from HBP bind poly(rG) and, at a much lower level, single-stranded and double-stranded DNA. Thus, single KH domains are discrete and independent nucleic-acid-binding units. Moreover, different KH domains bind different nucleic acids, suggesting that KH domains are composed of a conserved, weakly nucleic-acid-binding, structure that is fine tuned, by sequence variation, resulting in sequencespecific nucleic-acid-binding entities.

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“…The in vitro GST-SH2D1A binding proteins p160, p130, and p115 were identified as ␣-coatomer (24), hnRNPU (25) or GAPII, and nucleolin C23 (26) or Eps15R (17), respectively. The association of FLAG-SH2D1A with Eps15R could not be detected with anti-Eps15R antibodies.…”

Section: Dok1mentioning

confidence: 99%

The X-linked lymphoproliferative syndrome gene product SH2D1A associates with p62^dok(Dok1) and activates NF-κB

Sylla

Murphy

Cahir-McFarland³

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

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The X-linked lymphoproliferative syndrome (XLP) is a genetic disorder in which affected males have a morbid or fatal response to Epstein-Barr virus infection. The XLP deficiency has been mapped to a gene encoding a 128-residue protein, SH2D1A, which is comprised principally of a Src homology 2 (SH2) domain. We now report that SH2D1A associates with Dok1, a protein that interacts with Ras-GAP, Csk, and Nck. An SH2D1A SH2 domain mutant that has been identified in XLP does not associate with Dok1, in accord with the hypothesis that this interaction is linked to XLP. The association of SH2D1A with Dok1 also depends on phosphorylation of Dok1 Y 449 in the sequence ALYSQVQK. Further, overexpression of SH2D1A is found to activate NF-B in 293T cells. NF-B activation by SH2D1A does not depend on the wild-type SH2 domain and is inhibited by a dominant-negative I B kinase ␤. Thus, SH2D1A can affect multiple intracellular signaling pathways that are potentially important in the normal effective host response to Epstein-Barr virus infection. Epstein-Barr virus ͉ genetic disease

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Cloning and sequencing of the human nucleolin cDNA

Cited by 130 publications

References 36 publications

Domain Structure of Human Nuclear DNA Helicase II (RNA Helicase A)

Domain Structure of Human Nuclear DNA Helicase II (RNA Helicase A)

Characterisation of the Nucleic‐Acid‐Binding Activity of KH Domains Different Properties of Different Domains

The X-linked lymphoproliferative syndrome gene product SH2D1A associates with p62^dok(Dok1) and activates NF-κB

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Cloning and sequencing of the human nucleolin cDNA

Cited by 130 publications

References 36 publications

Domain Structure of Human Nuclear DNA Helicase II (RNA Helicase A)

Domain Structure of Human Nuclear DNA Helicase II (RNA Helicase A)

Characterisation of the Nucleic‐Acid‐Binding Activity of KH Domains Different Properties of Different Domains

The X-linked lymphoproliferative syndrome gene product SH2D1A associates with p62dok(Dok1) and activates NF-κB

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The X-linked lymphoproliferative syndrome gene product SH2D1A associates with p62^dok(Dok1) and activates NF-κB