Retroviral Recombination and Reverse Transcription

Hu, Wei-Shau; Temin, Howard M.

doi:10.1126/science.1700865

Cited by 551 publications

(457 citation statements)

References 20 publications

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“…To exclude the possibility that the LTR repair was occurring during reverse transcription, 24,25 vector plasmid DNAs containing the CCCACCC motif or its mutant RA-ml form were recovered 42 h after transfection. Unintegrated plasmid DNA was recovered from step 1 C3A2 packaging cells and transformed into the recombination-deficient E. coli host strain SOLR.…”

Section: Experimental Systemmentioning

confidence: 99%

Capture of a recombination activating sequence from mammalian cells

Olson

Dornburg

1999

Gene Ther

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We have developed a genetic trap for identifying revealed a putative recombination signal (CCCACCC). sequences that promote homologous DNA recombination.When this heptamer or an abbreviated form (CCCACC) The trap employs a retroviral vector that normally disables were reinserted into the vector, they stimulated vector itself after one round of replication. Insertion of defined repair and other DNA rearrangements. Mutant forms of DNA sequences into the vector induced the repair of a 300 these oligomers (eg CCCAACC or CCWACWS) did not. base pair deletion, which restored its ability to replicate.Our data suggest that the recombination events occurred Tests of random sequence libraries made in the vector within 48 h after transfection.

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Section: Experimental Systemmentioning

confidence: 99%

Capture of a recombination activating sequence from mammalian cells

Olson

Dornburg

1999

Gene Ther

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“…Recent evidence shows that complete proviral DNA synthesis occurs using only one of the copackaged RNA templates (Jones ef a/., 1994). Although there are two copies of genomic RNA within each retrovirus particle thus enabling the possible generation of two independent copies of preintegrated proviral DNA, only a single provirus is generated per infection (Panganiban and Fiore, 1988;Hu and Temin, 1990). The viral encoded RT plays a key role in this complex replication cycle.…”

Section: Replication Of the Viral Genomementioning

confidence: 99%

“…As soon as the 3' end is replicated beyond the tRNA primer, the RNase H removes the rest of the tRNA at the 5' end of the minus-strand (Figure 1, step 8). A second switch transfers the growing plus-strand DNA from the 5' end to the 3' end of the same molecule of newly synthesized minusstrand DNA (Panganiban and Fiore, 1988;Hu and Temin, 1990). This intramolecular process leads to the generation of a circular molecule (Withcomb et al, 1990;Figure 1, step 9).…”

Section: Plus-strand Dna Synthesismentioning

confidence: 99%

“…After strong-stop minusstrand DNA synthesis template switching occurs. This switch transfers the growing DNA minus-strand from the 5' end of the RNA molecule to the 3 1 end of the same, or a second RNA molecule (Panganiban and Fiore, 1988;Hu and Temin, 1990; Figure 1, step 4). This process is favoured by the redundant LTR.…”

Section: Minus-strand Dna Synthesismentioning

confidence: 99%

“…In accepted models of reverse transcription (Boone and Skalka, 1981;Panganiban and Fiore, 1988;Hu and Temin, 1990) the origin of the minus-strand is determined by a tRNA molecule that is copackaged with the viral genomic RNA and is hybridized near the 5' end (Figure 1, step 1). This region defines the 3' boundary of the long terminal repeat (LTR) and is the called primer binding site (PBS).…”

Section: Minus-strand Dna Synthesismentioning

confidence: 99%

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Review

1996

Biological Chemistry Hoppe-Seyler

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Proteolytic enzymes have many physiological functions in plants, bacteria, viruses, protozoa and mammals. They play a role in processes such as food digestion, complement activation or blood coagulation. The action of proteolytic enzymes is biologically controlled by proteinase inhibitors and increasing attention is being paid to the physiological significance of these natural inhibitors in pathological processes. The reason for this growing interest is that uncontrolled proteolysis can lead to irreversible damage e.g. in chronic inflammation or tumor metastasis. This review focusses on the possible role of the cystatins, natural and specific inhibitors of the cysteine proteinases, in pathological processes. Key words: Cystatins / Cysteine proteinases / Inflammation / Inhibitors / Pathological processes. Cysteine ProteinasesCysteine Proteinases, synonymous with thiol proteinases, are small proteins with molecular masses varying from 23 to 24 kDa and with two catalytic residues, Cys25 and His159, which are involved in the hydrolytic reaction. Cysteine proteinases catalyze the hydrolysis of various polypeptide substrates and are most active under reducing and mildly acidic conditions (pH 5 -6.5). They have been detected in and isolated from a large number of biological sources including plants, bacteria, animals and humans. Bacterial cysteine proteinases are produced by Clostridium histolyticum, named clostripain, by hemolytic group A streptococci and by the pathogenic anaerobic Porphyromonas gingivalis, a bacterium associated with periodontitis. Bacterial cysteine proteinases probably play a role in the penetration of normal tissues by the bacteria and in the food digestion. Viral cysteine proteinases from picornaviruses, e.g. the poliovirus and rhinovirus type I, are involved in proteolytic cleavage of precursor proteins for virus replication and for the production of new virus particles. A virus-coded cysteine proteinase is involved in this process (Kay and Dunn, 1990; Körant et a/., 1985;. HIV-I also needs proteolytic processing by cysteine proteinases to regulate the expression of viral proteins (Guy ef a/., 1991). Protozoal cysteine proteinases are produced by a number of protozoan parasites to facilitate host invasion, metabolize host proteins, to degrade the host immune molecules or to use them for intracellular replication. Cysteine proteinases are produced by e.g. Trypanosoma cruzi, the causative agent of American trypanosomiasis or by Leishmania species, causing one of the six major parasitic diseases. Furthermore, human malarial parasites produce a broad scala of proteinases including cysteine proteinase which are involved in erythrocyte invasion and rupture (McKerrow, 1993). Mammalian cysteine proteinases are present in the lysosomes of cells. Lysosomes contain different cysteine proteinases, the most important being the cathepsins B, H, L and S Kirschke, 1981, Barrett et a/., 1988). These cathepsins have common ancestors and are related to papain. Cathepsin B has been detected in every tissue or cel...

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Molecular Targets of Gene Transfer Therapy for HIV Infection

Buchschacher

1993

JAMA

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Retroviral Recombination and Reverse Transcription

Cited by 551 publications

References 20 publications

Capture of a recombination activating sequence from mammalian cells

Capture of a recombination activating sequence from mammalian cells

Review

Molecular Targets of Gene Transfer Therapy for HIV Infection

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