Nucleic acid binding properties of the nucleic acid chaperone domain of hepatitis delta antigen

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Nucleic acid binding properties of the nucleic acid chaperone domain of hepatitis delta antigen.

The N terminal region of hepatitis delta antigen (HDAg), referred to here as NdAg, has a nucleic acid chaperone activity that modulates the ribozyme activity of hepatitis delta virus (HDV) RNA and stimulates hammerhead ribozyme catalysis. We characterized the nucleic acid binding properties of NdAg, identified the structural and sequence domains important for nucleic acid binding, and studied t...

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Nucleic-acid-binding properties of the C2-L1Tc nucleic acid chaperone encoded by L1Tc retrotransposon

It has been reported previously that the C2-L1Tc protein located in the Trypanosoma cruzi LINE (long interspersed nuclear element) L1Tc 3' terminal end has NAC (nucleic acid chaperone) activity, an essential activity for retrotransposition of LINE-1. The C2-L1Tc protein contains two cysteine motifs of a C2H2 type, similar to those present in TFIIIA (transcription factor IIIA). The cysteine moti...

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Structural and nucleic acid binding properties of hepatitis delta virus small antigen

AIM To further characterize the structure and nucleic acid binding properties of the 195 amino acid small delta antigen, S-HDAg, a study was made of a truncated form of S-HDAg, comprising amino acids 61-195 (∆60HDAg), thus lacking the domain considered necessary for dimerization and higher order multimerization. METHODS Circular dichroism, and nuclear magnetic resonance experiments were used ...

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Nucleic acid binding and chaperone properties of HIV-1 Gag and nucleocapsid proteins

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ژورنال

عنوان ژورنال: Nucleic Acids Research

سال: 2003

ISSN: 1362-4962

DOI: 10.1093/nar/gkg857