Author

Poppe

Date of Award

12-1989

Degree Name

Master of Arts

Department

Biological Sciences

First Advisor

Dr. Gyula Ficsor

Second Advisor

Dr. Karim Essani

Third Advisor

Dr. W. Gary Tarpley

Access Setting

Masters Thesis-Open Access

Abstract

The human immunodeficiency virus (HIV) is the etiological agent of the acquired immune deficiency syndrome (AIDS). This retrovirus, encodes a RNA dependent DNA polymerase, reverse transcriptase (RT), which is essential to virus replication. Biochemical analysis indicated that RT is composed of 2 polypeptides of 66,000 and 51,000 daltons (p66 and p51) which combine to form a heterodimer. This heterodimer is thought to arise from the post-translational processing where p66 is made and either autocatalytic or proteolytic cleavage events result in a heterogeneous p66/p51. Site-directed mutagenesis was used at the proposed processing site to probe HIV-RT processing.

Three prokaryotic expression vectors each carrying a mutated form of RT were constructed. These mutants were induced and the product evaluated for RT enzymatic activity and the forms of RT protein visualized on SDS polyacrylamide gels and western blots. Results suggest that the mutations were at or near the RT processing site.

Included in

Biology Commons

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