BIOPHYSICAL STUDIES OF RETROVIRAL NUCLEIC ACID INTERACTIVE PROTEINS: HIV

HIV-1的核衣壳(NC)蛋白p7是 基因组RNA的包装。该蛋白质(55个残基)含有两个锌 手指和一个与核酸有关的Trp残基 通过与碱基的堆积相互作用而结合。我们有 表征了金属的寿命和动态各向异性特性 自由并与各种二价离子(锌、镉、二氧化碳)和铟结合 与DNA和RNA寡核苷酸的复合体。TRP的摄动 正在研究寡核苷酸结合时的荧光团 提供了插层芳烃残基相互作用的模型 有了核酸晶格。一系列截断和点突变 序列已经被用来表明存在瞬时相互作用 其中两个锌指紧靠在一起。这些研究 正在延伸到其他HIV-1蛋白(逆转录 整合酶)以及从不同来源分离的核衣壳蛋白 逆转录病毒(SIV、HTLV-1)

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)