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Vaccinia NPH-I, a DExH-box ATPase, is the energy coupling factor for mRNA transcription termination.
TLDR
NPH-I serves two roles in transcription: it acts in concert with VTF/CE to catalyze release of UUUUUNU-containing nascent RNA from the elongation complex, and it acts by itself as a polymerase elongation factor to facilitate readthrough of intrinsic pause sites. Expand
Phylogeny of mRNA capping enzymes.
TLDR
A structure-function analysis of the six motifs performed by targeted mutagenesis of Ceg1, the Saccharomyces cerevisiae guanylyltransferase allowed us to identify the capping enzyme of Caenorhabditis elegans and identify the structural basis for covalent catalysis. Expand
Factor-dependent Release of Nascent RNA by Ternary Complexes of Vaccinia RNA Polymerase*
TLDR
It is demonstrated that ternary complexes are refractory to VTF-mediated transcript release when the first U of the UUUUUNU signal is situated 20 nucleotides from the growing point of the nascent chain. Expand
Defective Binding of Neutral Lipids by a Carboxyl-terminal Deletion Mutant of Cholesteryl Ester Transfer Protein
TLDR
The studies suggest that amino acids 470-475 (forming part of a COOH-terminal amphipathic helix) are involved in CE and TG binding by CETP but are not required either for the binding of PC by CETp or the association of CETP with HDL. Expand
The D1 and D12 subunits are both essential for the transcription termination factor activity of vaccinia virus capping enzyme
TLDR
Both full-length subunits are required for transcription termination in vaccinia virus mRNA capping enzyme, a heterodimer of 95- and 33-kDa subunits encoded by the D1 and D12 genes, respectively. Expand
A role for the H4 subunit of vaccinia RNA polymerase in transcription initiation at a viral early promoter.
  • L. Deng, S. Shuman
  • Medicine, Biology
  • The Journal of biological chemistry
  • 13 May 1994
TLDR
It is suggested that H4 functions as a molecular bridge to ETF and thereby allows specific recognition of early promoters by the core RNA polymerase after the elongation complex is established. Expand
An ATPase Component of the Transcription Elongation Complex Is Required for Factor-dependent Transcription Termination by Vaccinia RNA Polymerase*
  • L. Deng, S. Shuman
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • 15 November 1996
TLDR
It is proposed that factor X, which has an associated DNA-dependent ATPase activity, mediates the requirement for ATP hydrolysis during transcription termination, and restored VTF responsiveness to heparin-stripped ternary complexes. Expand
Identification of a sequence within the C-terminal 26 amino acids of cholesteryl ester transfer protein responsible for binding a neutralizing monoclonal antibody and necessary for neutral lipid
TLDR
Six deletion mutants between Arg-451 and Leu-475 are generated by in vitro mutagenesis and expressed mutant proteins in mammalian cells, suggesting a direct involvement in neutral lipid transfer. Expand
Point mutagenesis of carboxyl-terminal amino acids of cholesteryl ester transfer protein. Opposite faces of an amphipathic helix important for cholesteryl ester transfer or for binding neutralizing
TLDR
It is concluded that the hydrophobic face of a carboxyl-terminal helix of CETP is directly involved in the mechanism of CE transfer, and that TP2 inhibits activity by local sterical hindrance. Expand
Structure-function analysis of the triphosphatase component of vaccinia virus mRNA capping enzyme
TLDR
It is reported that GppppA-capped RNA is a poor substrate for cap methylation by the vaccinia virus and Saccharomyces cerevisiae RNA (guanine-7) methyltransferases. Expand
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