The interaction of nucleocapsid protein, a reverse transcription accessory factor, with replication primer transfer RNA /
(residues 1 1 1) and the zinc-finger cooperate to alter the
| Main Author: | |
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| Format: | Thesis eBook |
| Language: | English |
| Published: |
[Place of publication not identified] :
[publisher not identified] ;
1994.
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| Subjects: | |
| Online Access: | Link to OAKTrust copy |
| Summary: | (residues 1 1 1) and the zinc-finger cooperate to alter the 32p labelled yeast tRNAPhe shows that HIV-1 NC changes the abilities to inhibit the cleavage. The data taken together activity, consistent with a 1:1 stoichiometry. A number of Aimed at understanding the initiation of reverse appears to have a far greater reactivity toward the single between the transfer RNA primer and a complementary genomic binding by NC and the identification of the functional chemical modification and/or have either or both N- or C- cleavage is completely inhibited. From examination of an conformation of the tRNAPhe molecule such that the lead conformation of TRNA. currently being used to determine the molecular details of domains of NC required for productive binding to TRNA. A found that HIV-1 NC and tRNAPhe mixed at a 0.5 to 1:1 ratio have one or both zinc-fingers destroyed by mutagenesis or high yield of protein. The Mason-Pfizer monkey virus HIV-1 NC-concentration dependence of this reaction, it is immunodeficiency virus type 1 nucleocapsid protein (HIV-1 NC) In the initiation of reverse transcription in animal Investigation of the lead-catalyzed auto-cleavage of the 5'- is sufficient to completely suppress the observable cleavage labelled Mg2+-tRNAHis in the presence and absence of human nucleocapsid protein (MPMV NC) and 15N-labelled MPMV NC are particularly efficient and relatively easy purification previous methodology is outlined and gives high purity and protocol for NC proteins which avoids denaturation steps of recombinant nucleocapsid proteins, the determination of the retroviruses, an obligate step is the formation of RNA duplex RNA sequence, termed the primer binding site (PBS). A shown to be required for this step in vitro and in vivo. shows that the 3'-end acceptor stem of the NC-TRNA complex strand-specific RNase than that of the uncomplexed TRNA. structural changes induced in a model TRNA as a result of substitution and domain deletion mutants of HIV-1 NC which suggest the possibility that the N-terminal domain region terminal flanking region deleted have been examined for their the protein structure. An RNase Tl digestion of 3,-32p transcription, this work describes the purification of virally encoded protein, nucleocapsid protein (NC), has been |
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| Item Description: | "Major subject: Biochemistry". Vita. |
| Physical Description: | viii, 83 leaves : illustrations ; 28 cm. Also available online. |
| Bibliography: | Includes bibliographical references. |