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Abstract
DNA BINDING FUNCTION AND POLYMERASE ACTIVITY OF THE P51 SUBUNIT OF HIV-1 RT ARE STIMULATED IN THE PRESENCE OF 15 KDA RNASE FRAGMENT
V. Pandey, A. Upadhyay
Department of Biochemistry and Molecular Biology, Center for the Study of Emerging and Re-Emerging Pathogens, UMDNJ-New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA
The p51 subunit of HIV-1 RT exists as a monomer and is catalytically inactive. We observed that polymerase activity of p51 is significantly stimulated when supplemented with RNase H fragment. Similarly, RNA cleavage activity of the inactive RNAse H fragment is partially restored in the presence of p51. We postulate that p51 and RNase H fragment may physically interact to mimic a putative conformation similar to the monomeric p66, which may dimerize with another p51 subunit to assume a heterodimeric like structure. This contention is supported by our observation that DNA binding function of p51 is significantly stimulated in the presence of increasing concentrations of RNase H. In the crystal structures of HIV-1 RT in apoform or in the binary and ternary complexes, the structure of the C-terminal region of the connection subdomain of p51 subunit spanning residues 421/430-440 is missing. The corresponding region in the connection subdomain of p66 subunit contains most of the hydrophobic interactions with the RNase H domain. This interaction may be essential for towing out the connection subdomain from the polymerase cleft during dimerization.
The 2nd IAS Conference on HIV Pathogenesis and Treatment
Abstract no.
311
Suggested Citation
" V. Pandey, et al.
DNA BINDING FUNCTION AND POLYMERASE ACTIVITY OF THE P51 SUBUNIT OF HIV-1 RT ARE STIMULATED IN THE PRESENCE OF 15 KDA RNASE FRAGMENT.
Poster:
The 2nd IAS Conference on HIV Pathogenesis and Treatment:
Abstract no.
311"
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