Sequence-specific interaction between HIV-1 matrix protein and viral genomic RNA revealed by in vitro genetic selection
| dc.contributor.author | Purohit, Aruna | |
| dc.contributor.author | Dupont, Stefan A. | |
| dc.contributor.author | Stevenson, Mario | |
| dc.contributor.author | Green, Michael R. | |
| dc.date | 2022-08-11T08:08:47.000 | |
| dc.date.accessioned | 2022-08-23T16:08:23Z | |
| dc.date.available | 2022-08-23T16:08:23Z | |
| dc.date.issued | 2001-05-10 | |
| dc.date.submitted | 2008-11-26 | |
| dc.identifier.citation | <p>RNA. 2001 Apr;7(4):576-84.</p> | |
| dc.identifier.issn | 1355-8382 (Print) | |
| dc.identifier.pmid | 11345436 | |
| dc.identifier.uri | http://hdl.handle.net/20.500.14038/32436 | |
| dc.description.abstract | The human immunodeficiency virus type-1 matrix protein (HIV-1 MA) is a multifunctional structural protein synthesized as part of the Pr55 gag polyprotein. We have used in vitro genetic selection to identify an RNA consensus sequence that specifically interacts with MA (Kd = 5 x 10(-7) M). This 13-nt MA binding consensus sequence bears a high degree of homology (77%) to a region (nt 1433-1446) within the POL open reading frame of the HIV-1 genome (consensus sequence from 38 HIV-1 strains). Chemical interference experiments identified the nucleotides within the MA binding consensus sequence involved in direct contact with MA. We further demonstrate that this RNA-protein interaction is mediated through a stretch of basic amino acids within MA. Mutations that disrupt the interaction between MA and its RNA binding site within the HIV-1 genome resulted in a measurable decrease in viral replication. | |
| dc.language.iso | en_US | |
| dc.relation | <p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11345436&dopt=Abstract">Link to article in PubMed</a></p> | |
| dc.relation.url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1370111/ | |
| dc.subject | Base Sequence; Binding Sites; Consensus Sequence; Directed Molecular Evolution; Gene Products, gag; Gene Products, pol; HIV Antigens; HIV-1; Molecular Sequence Data; Protein Binding; Protein Precursors; RNA, Viral; RNA-Binding Proteins; Sequence Homology, Nucleic Acid; T-Lymphocytes; *Viral Proteins; gag Gene Products, Human Immunodeficiency Virus | |
| dc.subject | Life Sciences | |
| dc.subject | Medicine and Health Sciences | |
| dc.title | Sequence-specific interaction between HIV-1 matrix protein and viral genomic RNA revealed by in vitro genetic selection | |
| dc.type | Journal Article | |
| dc.source.journaltitle | RNA (New York, N.Y.) | |
| dc.source.volume | 7 | |
| dc.source.issue | 4 | |
| dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/gsbs_sp/1006 | |
| dc.identifier.contextkey | 673222 | |
| html.description.abstract | <p>The human immunodeficiency virus type-1 matrix protein (HIV-1 MA) is a multifunctional structural protein synthesized as part of the Pr55 gag polyprotein. We have used in vitro genetic selection to identify an RNA consensus sequence that specifically interacts with MA (Kd = 5 x 10(-7) M). This 13-nt MA binding consensus sequence bears a high degree of homology (77%) to a region (nt 1433-1446) within the POL open reading frame of the HIV-1 genome (consensus sequence from 38 HIV-1 strains). Chemical interference experiments identified the nucleotides within the MA binding consensus sequence involved in direct contact with MA. We further demonstrate that this RNA-protein interaction is mediated through a stretch of basic amino acids within MA. Mutations that disrupt the interaction between MA and its RNA binding site within the HIV-1 genome resulted in a measurable decrease in viral replication.</p> | |
| dc.identifier.submissionpath | gsbs_sp/1006 | |
| dc.contributor.department | Program in Gene Function and Expression | |
| dc.contributor.department | Program in Molecular Medicine | |
| dc.contributor.department | Graduate School of Biomedical Sciences | |
| dc.contributor.department | Graduate School of Biomedical Sciences | |
| dc.source.pages | 576-84 |
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