| Title | HIV-1 Rev is highly mutable and glycine substitution of R35 allows mutation of N40 / by Elite Joseph Possik | Thesis |
| Name(s) | Possik, Elite Joseph (Main Author)
American University of Beirut. Faculty of Arts and Sciences. Department of Biology (Related name)
|
| Publication | 2009
|
| Link(s) | Click for full-text
|
| Physical Details | xvii, 98 leaves; ill. (some col.); 30 cm.
|
| Subjects | HIV (Viruses)
Viruses--Evolution
RNA-protein interactions
Glycine
Biochemistry
Arginine
|
| Classmarks | T:005291
|
| Notes | Dissertation: Thesis (M.S.)--American University of Beirut, Dept. of Biology, 2009.
Dissertation: Advisor : Dr. Colin Smith, Assistant Professor, Biology
Member of Committee : Dr. Mike Osta, Assistant Professor, Biology
Member of Committee : Dr. Rabih Talhouk, Professor, Biology.
General: Appendix : leaves 84-87.
Bib. & Index: Bibliography : leaves 88-98.
|
| Abstract | The arginine-rich domain of the HIV-1 Rev protein binds to a short stem in the Rev Response Element (RRE) RNA and mediates the export of incompletely-spliced viral transcripts. Rev-RRE recognition regulates gene expression and is essential for viral replication. Many biochemical, genetic, and structural studies of Rev-RRE have been published, yet the roles of several amino acids in binding are still unclear. Randomized libraries of the arginine-rich domain of Rev were constructed and assayed for their ability to bind RREIIB using a bacterial reporter system based on bacteriophage lambda N antitermination. The results reveal Rev34-48 is highly mutable, support specific biochemical roles for certain residues, and provide biochemical support to the existing NMR-based structural model. These results are strikingly similar to the sequence variability found in clinical isolates, suggesting that the wild HIV population is exploring all possible evolutionary paths. The high proportion of active mutants supports the neutral theory of molecular evolution. Selection of N40 mutants serendipitously revealed R35G mutants that allow mutation of an asparagine at position 40. That a distinct binding strategy occurs with only two mutations highlights the ability of arginine-rich peptides to evolve new recognition strategies.
|
| Availability | |
| | Barcode |
Location |
Shelf |
Shelfmark |
Status |
Category | | | Jafet Archives and Special Collections | Thesis | T:5291:c.1 | ASC-Binding | Building Use |
|
 |
|
|
© Fretwell-Downing Informatics
|
|
|
