Liao, H. J., Kobayashi, R., Mathews, M. B. (July 1998) Activities of adenovirus virus-associated RNAs: purification and characterization of RNA binding proteins. Proceedings of the National Academy of Sciences, 95 (15). pp. 8514-9. ISSN 0027-8424 (Print)
Preview |
PDF
Liao_PNAS_1998.pdf - Published Version Download (317kB) | Preview |
Abstract
Most human adenoviruses encode two virus-associated (VA) RNAs, VA RNAI and VA RNAII, that accumulate to high levels in the cytoplasm of infected cells. The function of VA RNAI in blocking the activation of the cellular kinase PKR is well known, but the role of VA RNAII is obscure. Herein we characterize and purify several human proteins that interact preferentially with VA RNAII in Northwestern blot assays. Two of these proteins were identified as RNA helicase A and NF90, a component of the heterodimeric nuclear factor of activated T cells (NFAT). They copurified with the smaller NFAT subunit, NF45, which did not bind VA RNAII, and with an unidentified protein, p97, which did bind VA RNAII. Both RNA helicase A and NF90 contain two copies of a double-stranded (ds) RNA binding motif and bind strongly to dsRNA. NF90 interacts with RNAs in the following order of affinity: dsRNA > VA RNAII > VA RNAI > single-stranded RNA. Furthermore, VA RNAII is more effective than VA RNAI as an inhibitor of RNA helicase activity. These data identify RNA helicase A and NF90 as cellular proteins with an affinity for dsRNA and other structured RNA molecules and suggest that their functions are subject to regulation by RNA ligands including VA RNAII.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | Adenoviridae/ genetics Amino Acid Sequence Blotting, Northern Blotting, Western Cell Line DNA-Binding Proteins/chemistry/isolation & purification/metabolism Humans Molecular Sequence Data NFATC Transcription Factors Nuclear Factor 45 Protein Nuclear Factor 90 Proteins Nuclear Proteins RNA Helicases RNA Nucleotidyltransferases/chemistry/isolation & purification/metabolism RNA, Viral/ genetics/metabolism RNA-Binding Proteins/chemistry/ isolation & purification/metabolism Research Support, U.S. Gov't, P.H.S. Transcription Factors/chemistry/isolation & purification/metabolism |
| Subjects: | organs, tissues, organelles, cell types and functions > cell types and functions > cell types > T cells organs, tissues, organelles, cell types and functions > cell types and functions > cell types > T cells organs, tissues, organelles, cell types and functions > cell types and functions > cell types > T cells organism description > virus > adenovirus bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > helicase bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > RNA binding protein bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor |
| CSHL Authors: | |
| Communities: | CSHL labs > Kobayashi lab |
| Depositing User: | Kathleen Darby |
| Date: | 21 July 1998 |
| Date Deposited: | 01 May 2014 16:24 |
| Last Modified: | 11 Sep 2019 15:32 |
| PMCID: | PMC21107 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/29907 |
Actions (login required)
 |
Administrator's edit/view item |