Back to Search
Start Over
Polymerase translocation with respect to single-stranded nucleic acid: looping or wrapping of primer around a poly(A) polymerase.
- Source :
-
Structure (London, England : 1993) [Structure] 2009 May 13; Vol. 17 (5), pp. 680-9. - Publication Year :
- 2009
-
Abstract
- Vaccinia virus protein VP55 translocates continuously with respect to single-stranded nucleic acid while extending its 3'end. Here, all key sites of polymerase-primer interaction were identified, demonstrating the wrapping or looping of polyadenylation primer around the polymerase during translocation. Side-chain substitutions at one of the sites indicated its requirement for tail extension beyond approximately 12 nucleotides in length, and conformational changes observed upon oligonucleotide binding suggested allosteric connectivity during translocation. Conformational changes in VP39 upon VP55 binding suggested that, within the VP55-VP39 complex, VP39's mRNA 5' cap binding site closes. The crystallographic structure showed a PAPase catalytic center without side-chain substitutions, possessing two metal ions and with all known reactive and catalytic groups represented, fitting a classical two-metal ion mechanism for phosphoryl transfer.
- Subjects :
- Base Sequence
Binding Sites
Models, Molecular
Molecular Sequence Data
Polynucleotide Adenylyltransferase metabolism
Protein Conformation
RNA metabolism
RNA Cap-Binding Proteins chemistry
RNA Cap-Binding Proteins metabolism
RNA Caps chemistry
RNA Caps metabolism
RNA, Viral chemistry
RNA, Viral metabolism
Vaccinia virus metabolism
Viral Proteins metabolism
Polynucleotide Adenylyltransferase chemistry
RNA chemistry
Viral Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0969-2126
- Volume :
- 17
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Structure (London, England : 1993)
- Publication Type :
- Academic Journal
- Accession number :
- 19446524
- Full Text :
- https://doi.org/10.1016/j.str.2009.03.012