PubTransformer

A site to transform Pubmed publications into these bibliographic reference formats: ADS, BibTeX, EndNote, ISI used by the Web of Knowledge, RIS, MEDLINE, Microsoft's Word 2007 XML.

Poliovirus protein 3AB displays nucleic acid chaperone and helix-destabilizing activities.

Abstract Poliovirus protein 3AB displayed nucleic acid chaperone activity in promoting the hybridization of complementary nucleic acids and destabilizing secondary structure. Hybridization reactions at 30 degrees C between 20- and 40-nucleotide RNA oligonucleotides and 179- or 765-nucleotide RNAs that contained a complementary region were greatly enhanced in the presence of 3AB. The effect was nonspecific as reactions between DNA oligonucleotides and RNA or DNA templates were also enhanced. Reactions were optimal with 1 mM MgCl(2) and 20 mM KCl. Analysis of the reactions with various 3AB and template concentrations indicated that enhancement required a critical amount of 3AB that increased as the concentration of nucleic acid increased. This was consistent with a requirement for 3AB to "coat" the nucleic acids for enhancement. The helix-destabilizing activity of 3AB was tested in an assay with two 42-nucleotide completely complementary DNAs. Each complement formed a strong stem-loop (DeltaG = -7.2 kcal/mol) that required unwinding for hybridization to occur. DNAs were modified at the 3' or 5' end with fluorescent probes such that hybridization resulted in quenching of the fluorescent signal. Under optimal conditions at 30 degrees C, 3AB stimulated hybridization in a concentration-dependent manner, as did human immunodeficiency virus nucleocapsid protein, an established chaperone. The results are discussed with respect to the role of 3AB in viral replication and recombination.
PMID
Related Publications

Genetic dissection of interaction between poliovirus 3D polymerase and viral protein 3AB.

Tyrosine 3 of poliovirus terminal peptide VPg(3B) has an essential function in RNA replication in the context of its precursor protein, 3AB.

HIV-1 nucleocapsid protein as a nucleic acid chaperone: spectroscopic study of its helix-destabilizing properties, structural binding specificity, and annealing activity.

The identification and characterization of nucleic acid chaperone activity of human enterovirus 71 nonstructural protein 3AB.

The twenty-nine amino acid C-terminal cytoplasmic domain of poliovirus 3AB is critical for nucleic acid chaperone activity.

Authors

Mayor MeshTerms

Molecular Chaperones

Keywords
Journal Title journal of virology
Publication Year Start




PMID- 16439523
OWN - NLM
STAT- MEDLINE
DA  - 20060127
DCOM- 20060224
LR  - 20150317
IS  - 0022-538X (Print)
IS  - 0022-538X (Linking)
VI  - 80
IP  - 4
DP  - 2006 Feb
TI  - Poliovirus protein 3AB displays nucleic acid chaperone and helix-destabilizing
      activities.
PG  - 1662-71
AB  - Poliovirus protein 3AB displayed nucleic acid chaperone activity in promoting the
      hybridization of complementary nucleic acids and destabilizing secondary
      structure. Hybridization reactions at 30 degrees C between 20- and 40-nucleotide 
      RNA oligonucleotides and 179- or 765-nucleotide RNAs that contained a
      complementary region were greatly enhanced in the presence of 3AB. The effect was
      nonspecific as reactions between DNA oligonucleotides and RNA or DNA templates
      were also enhanced. Reactions were optimal with 1 mM MgCl(2) and 20 mM KCl.
      Analysis of the reactions with various 3AB and template concentrations indicated 
      that enhancement required a critical amount of 3AB that increased as the
      concentration of nucleic acid increased. This was consistent with a requirement
      for 3AB to "coat" the nucleic acids for enhancement. The helix-destabilizing
      activity of 3AB was tested in an assay with two 42-nucleotide completely
      complementary DNAs. Each complement formed a strong stem-loop (DeltaG = -7.2
      kcal/mol) that required unwinding for hybridization to occur. DNAs were modified 
      at the 3' or 5' end with fluorescent probes such that hybridization resulted in
      quenching of the fluorescent signal. Under optimal conditions at 30 degrees C,
      3AB stimulated hybridization in a concentration-dependent manner, as did human
      immunodeficiency virus nucleocapsid protein, an established chaperone. The
      results are discussed with respect to the role of 3AB in viral replication and
      recombination.
FAU - DeStefano, Jeffrey J
AU  - DeStefano JJ
AD  - Department of Cell Biology and Molecular Genetics, University of Maryland-College
      Park, Building 231, College Park, MD 20742, USA. [email protected]
FAU - Titilope, Oduyebo
AU  - Titilope O
LA  - eng
GR  - R01 GM051140/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Coenzymes)
RN  - 0 (Molecular Chaperones)
RN  - 0 (Oligonucleotides)
RN  - 0 (Viral Proteins)
RN  - 63231-63-0 (RNA)
RN  - 9007-49-2 (DNA)
SB  - IM
MH  - Coenzymes
MH  - DNA/chemistry/*metabolism
MH  - Enzyme Stability
MH  - *Molecular Chaperones
MH  - Nucleic Acid Conformation
MH  - Nucleic Acid Hybridization
MH  - Oligonucleotides/metabolism
MH  - Poliovirus/*physiology
MH  - RNA/chemistry/*metabolism
MH  - Substrate Specificity
MH  - Temperature
MH  - Viral Proteins/*physiology
PMC - PMC1367131
OID - NLM: PMC1367131
EDAT- 2006/01/28 09:00
MHDA- 2006/02/25 09:00
CRDT- 2006/01/28 09:00
AID - 80/4/1662 [pii]
AID - 10.1128/JVI.80.4.1662-1671.2006 [doi]
PST - ppublish
SO  - J Virol. 2006 Feb;80(4):1662-71.

<?xml version="1.0" encoding="UTF-8"?>
<b:Sources SelectedStyle="" xmlns:b="http://schemas.openxmlformats.org/officeDocument/2006/bibliography"  xmlns="http://schemas.openxmlformats.org/officeDocument/2006/bibliography" >
</b:Sources>