Vaccinia virus RNA helicase: Directionality and substrate specificity Journal Article
| Author: | Shuman, S. |
| Article Title: | Vaccinia virus RNA helicase: Directionality and substrate specificity |
| Abstract: | Vaccinia virus RNA helicase (NPH-II) catalyzes unidirectional unwinding of 3′-tailed duplex RNAs in the presence of a divalent cation and any one of the eight common nucleoside triphosphates (NTP). The helicase binds stably to the tailed RNA in the absence of any cofactor; strand displacement by the bound protein is coupled to NTP hydrolysis. Although the helicase is capable of binding to tailed duplex DNA as well as to tailed RNA, the enzyme is unable to unwind duplex DNA. It is suggested that NTP hydrolysis by RNA-bound NPH-II drives processive translocation of the protein in a 3′ to 5′ direction along the RNA strand, whereas energy utilization by DNA-bound enzyme leads to dissociation without extensive protein movement. A role for the RNA helicase in vaccinia mRNA synthesis is proposed. |
| Keywords: | controlled study; nonhuman; comparative study; protein binding; structure-activity relationship; double stranded dna; molecular sequence data; kinetics; messenger rna; virus rna; rna synthesis; substrate specificity; protein transport; vaccinia virus; base sequence; helicase; dna, single-stranded; dna binding; enzyme specificity; adenosine triphosphatase; enzyme binding; rna helicases; hydrolysis; rna, double-stranded; divalent cation; oligodeoxyribonucleotides; vaccinia; nucleoside triphosphate; virion; rna nucleotidyltransferases; priority journal; article; adenosinetriphosphatase |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 268 |
| Issue: | 16 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 1993-06-05 |
| Start Page: | 11798 |
| End Page: | 11802 |
| Language: | English |
| PUBMED: | 8505308 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 1 March 2019 -- Source: Scopus |
