The nucleocapsid (NC) protein p7 from HIV-1 is required for packaging of genomic RNA. The protein (55 residues) contains two zinc fingers and a single Trp residue that is involved in nucleic acid binding through stacking interactions with nucleobases. We have characterized the lifetime and dynamic anisotropy properties of metal free and bound to various divalent ions (Zn2+, Cd2+, Co2+) and in complexes with DNA and RNA oligonucleotides. Perturbations of the Trp fluorophore upon oligonucleotide binding are being investigated to provide a model for the interaction of intercalating aromatic residues with nucleic acid lattices. A series of truncated and point mutated sequences have been used to show that there is a transient interaction in which the two zinc fingers are in close proximity. These studies are being extended other HIV-1 proteins (reverse transcription integrase) as well as to nucleocapsid proteins isolated from different retroviruses (SIV, HTLV-1)

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR008119-07
Application #
6122890
Study Section
Project Start
1999-04-01
Project End
2000-03-31
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
7
Fiscal Year
1999
Total Cost
Indirect Cost
Name
University of Maryland Baltimore
Department
Type
DUNS #
003255213
City
Baltimore
State
MD
Country
United States
Zip Code
21201
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