Retroviral reverse transcriptases (other than those of HIV-1 and murine leukemia virus): A comparison of their molecular and biochemical properties

Hizi, Amnon; Herschhorn, Alon

doi:10.1016/j.virusres.2007.12.008

Cited by 31 publications

(37 citation statements)

References 151 publications

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“…The RT sequences reside within the pol coding domain. RTs from the different groups of retroviruses share similar activities but can differ in various parameters, such as: structure and subunit composition, molecular weights, catalytic properties, biochemical and biophysical characteristics and sensitivity to different inhibitors [1,2,7].…”

Section: Biogenesis Of Rtsmentioning

confidence: 99%

“…The RT of spumaviruses is generated from a separate spliced mRNA instead of the Gag-Pro-Pol polyprotein precursor, and infectious particles contain double-stranded DNA, similar to full length cDNA of the orthoretroviruses (see below). This suggests that RTN of spumaviruses takes place during the packaging of viral particles and before the virions enter the new target cells in a process reminiscent of the life cycle of hepadnaviruses [7][8][9]. Despite the clear separation between the pro and pol genes, there are some variations in the processing of RT by PR in different retroviral groups.…”

Section: Biogenesis Of Rtsmentioning

confidence: 99%

“…Obviously, cardinal contributions were also made prior to the identification of HIV in studies performed with other RTs, mainly those of murine leukemia virus (MLV) and avian sarcoma/leukemia virus (ASLV). A detailed review, written by us, that summarizes the unique properties of RTs other than those of HIV-1 and MLV can be found in the recent special issue dedicated to reverse transcriptase [7].…”

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confidence: 99%

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Retroviral reverse transcriptases

Herschhorn

Hizi

2010

Cell. Mol. Life Sci.

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107

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Reverse transcription is a critical step in the life cycle of all retroviruses and related retrotransposons. This complex process is performed exclusively by the retroviral reverse transcriptase (RT) enzyme that converts the viral single-stranded RNA into integration-competent double-stranded DNA. Although all RTs have similar catalytic activities, they significantly differ in several aspects of their catalytic properties, their structures and subunit composition. The RT of human immunodeficiency virus type-1 (HIV-1), the virus causing acquired immunodeficiency syndrome (AIDS), is a prime target for the development of antiretroviral drug therapy of HIV-1/AIDS carriers. Therefore, despite the fundamental contributions of other RTs to the understanding of RTs and retrovirology, most recent RT studies are related to HIV-1 RT. In this review we summarize the basic properties of different RTs. These include, among other topics, their structures, enzymatic activities, interactions with both viral and host proteins, RT inhibition and resistance to antiretroviral drugs.

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Section: Biogenesis Of Rtsmentioning

confidence: 99%

Section: Biogenesis Of Rtsmentioning

confidence: 99%

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confidence: 99%

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Retroviral reverse transcriptases

Herschhorn

Hizi

2010

Cell. Mol. Life Sci.

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107

111

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“…Other studies have also found these mutual IN-RT contacts in HIV-1 (15,(33)(34)(35). Moreover, in many alpharetroviruses, the IN sequence is part of two different proteins, the free IN molecule and the C terminus of the larger RT subunit (14,17,19). Also, we and others found that HIV-1 RT or HIV-1 RT-derived peptides could bind HIV-1 IN and affect its activities (33)(34)(35)41).…”

Section: Resultsmentioning

confidence: 78%

The Removal of RNA Primers from DNA Synthesized by the Reverse Transcriptase of the Retrotransposon Tf 1 Is Stimulated by Tf 1 Integrase

Herzig

Voronin

Hizi

2012

J Virol

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The Tf 1 retrotransposon represents a group of long terminal repeat retroelements that use an RNA self-primer for initiating reverse transcription while synthesizing the minus-sense DNA strand. Tf 1 reverse transcriptase (RT) was found earlier to generate the self-primer in vitro . Here, we show that this RT can remove from the synthesized cDNA the entire self-primer as well as the complete polypurine tract (PPT) sequence (serving as a second primer for cDNA synthesis). However, these primer removals, mediated by the RNase H activity of Tf 1 RT, are quite inefficient. Interestingly, the integrase of Tf 1 stimulated the specific Tf 1 RT-directed cleavage of both the self-primer and PPT, although there was no general enhancement of the RT's RNase H activity (and the integrase by itself is devoid of any primer cleavage). The RTs of two prototype retroviruses, murine leukemia virus and human immunodeficiency virus, showed only a partial and nonspecific cleavage of both Tf 1 -associated primers with no stimulation by Tf 1 integrase. Mutagenesis of Tf 1 integrase revealed that the complete Tf 1 integrase protein (excluding its chromodomain) is required for stimulating the Tf 1 RT primer removal activity. Nonetheless, a double mutant integrase that has lost its integration functions can still stimulate the RT's activity, though heat-inactivated integrase cannot enhance primer removals. These findings suggest that the enzymatic activity of Tf 1 integrase is not essential for stimulating the RT-mediated primer removal, while the proper folding of this protein is obligatory for this function. These results highlight possible new functions of Tf 1 integrase in the retrotransposon's reverse transcription process.

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“…Both MMTV and BLV RTs are transframe proteins encoded with a region spanning both the pro and pol genes. Unlike in BLV, where the pro-derived sequence of RT is absent in the protease carboxyl terminus, the C terminus of MMTV protease has a dual usage, also forming the N terminus of MMTV RT (15,16,21,29). It is possible that M-PMV RT, similar to RTs from MMTV and BLV, is also a transframe protein resulting from the processing of the Gag-Pro-Pol polyprotein.…”

mentioning

confidence: 99%

The G-Patch Domain of Mason-Pfizer Monkey Virus Is a Part of Reverse Transcriptase

Křížová

Hadravová

Štokrová

et al. 2012

J Virol

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Mason-Pfizer monkey virus (M-PMV), like some other betaretroviruses, encodes a G-patch domain (GPD). This glycine-rich domain, which has been predicted to be an RNA binding module, is invariably localized at the 3= end of the pro gene upstream of the pro-pol ribosomal frameshift sequence of genomic RNAs of betaretroviruses. Following two ribosomal frameshift events and the translation of viral mRNA, the GPD is present in both Gag-Pro and Gag-Pro-Pol polyproteins. During the maturation of the Gag-Pro polyprotein, the GPD transiently remains a C-terminal part of the protease (PR), from which it is then detached by PR itself. The destiny of the Gag-Pro-Pol-encoded GPD remains to be determined. The function of the GPD in the retroviral life cycle is unknown. To elucidate the role of the GPD in the M-PMV replication cycle, alanine-scanning mutational analysis of its most highly conserved residues was performed. A series of individual mutations as well as the deletion of the entire GPD had no effect on M-PMV assembly, polyprotein processing, and RNA incorporation. However, a reduction of the reverse transcriptase (RT) activity, resulting in a drop in M-PMV infectivity, was determined for all GPD mutants. Immunoprecipitation experiments suggested that the GPD is a part of RT and participates in its function. These data indicate that the M-PMV GPD functions as a part of reverse transcriptase rather than protease.

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Retroviral reverse transcriptases (other than those of HIV-1 and murine leukemia virus): A comparison of their molecular and biochemical properties

Cited by 31 publications

References 151 publications

Retroviral reverse transcriptases

Retroviral reverse transcriptases

The Removal of RNA Primers from DNA Synthesized by the Reverse Transcriptase of the Retrotransposon Tf 1 Is Stimulated by Tf 1 Integrase

The G-Patch Domain of Mason-Pfizer Monkey Virus Is a Part of Reverse Transcriptase

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