Authors: | Deng, L.; Shuman, S. |
Article Title: | Vaccinia NPH-I, a DExH-box ATPase, is the energy coupling factor for mRNA transcription termination |
Abstract: | Vaccinia virus RNA polymerase terminates transcription in response to a specific signal UUUUUNU in the nascent RNA. Transduction of this signal to the elongating polymerase requires a trans-acting viral termination factor (VTF/capping enzyme), and is coupled to the hydrolysis of ATP. Recent studies suggest that ATP hydrolysis is catalyzed by a novel termination protein (factor X), which is tightly associated with the elongation complex. Here, we identify factor X as NPH-I (nucleoside triphosphate phosphohydrolase-I), a virus-encoded DNA-dependent ATPase of the DExH-box family. We report that NPH-I serves two roles in transcription (1) it acts in concert with VTF/CE to catalyze release of UUUUUNU-containing nascent RNA from the elongation complex, and (2) it acts by itself as a polymerase elongation factor to facilitate readthrough of intrinsic pause sites. A mutation (K61A) in the GxGKT motif of NPH-I abolishes ATP hydrolysis and eliminates the termination and elongation factor activities. Related DExH proteins may have similar roles at postinitiation steps during cellular mRNA synthesis. |
Keywords: | signal transduction; controlled study; mutation; nonhuman; transcription, genetic; nucleoside triphosphatase; acid anhydride hydrolases; amino acid sequence; molecular sequence data; messenger rna; rna, messenger; recombinant proteins; vaccinia virus; heparin; models, genetic; adenosine triphosphate; adenosine triphosphatase; energy metabolism; adenosine triphosphatases; hydrolysis; rna transcription; viral proteins; rna polymerase; transcription termination; virus enzyme; nucleoside-triphosphatase; messenger rna synthesis; coupling factor; priority journal; article; nph-1 atpase; vaccina virus; terminator regions (genetics) |
Journal Title: | Genes and Development |
Volume: | 12 |
Issue: | 4 |
ISSN: | 0890-9369 |
Publisher: | Cold Spring Harbor Laboratory Press |
Date Published: | 1998-02-15 |
Start Page: | 538 |
End Page: | 546 |
Language: | English |
PUBMED: | 9472022 |
PROVIDER: | scopus |
PMCID: | PMC316528 |
DOI: | 10.1101/gad.12.4.538 |
DOI/URL: | |
Notes: | Article -- Export Date: 12 December 2016 -- Source: Scopus |