Cleavage of the HIV replication primer tRNALys,3 in human cells expressing bacterial anticodon nuclease

Nava Shterman; Orna Elroy-stein; Llan Morad; Michal Amitsur; Gabriel Kaufmann

doi:10.1093/nar/23.10.1744

Cleavage of the HIV replication primer tRNA^Lys,3 in human cells expressing bacterial anticodon nuclease

Nava Shterman, Orna Elroy-stein, Llan Morad, Michal Amitsur, Gabriel Kaufmann^*

^*Corresponding author for this work

Department of Cell Research and Immunology

Research output: Contribution to journal › Article › peer-review

Abstract

Anticodon nuclease is a bacterial restriction enzyme directed against tRNALv8. We report that anticodon nuclease also cleaves mammalian tRNA^Lys molecules, with preference and site specificity shown towards the natural substrate. Expression of the anticodon nuclease core polypeptide PrrC In HeLa cells from a recomblnant vaccinia virus elicited cleavage of intra-cellular tRNA^Lys,3The data justify an inquiry into the possible application of anticodon nuclease as an inhibitor of tRNA^Lys,3-primed HIV replication. They also indicate that the anticodon region of tRNA^Lys is a substrate recognition site and suggest that PrrC harbors the enzymatic activity.

Original language	English
Pages (from-to)	1744-1749
Number of pages	6
Journal	Nucleic Acids Research
Volume	23
Issue number	10
DOIs	https://doi.org/10.1093/nar/23.10.1744
State	Published - 25 May 1995

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title = "Cleavage of the HIV replication primer tRNALys,3 in human cells expressing bacterial anticodon nuclease",

abstract = "Anticodon nuclease is a bacterial restriction enzyme directed against tRNALv8. We report that anticodon nuclease also cleaves mammalian tRNALys molecules, with preference and site specificity shown towards the natural substrate. Expression of the anticodon nuclease core polypeptide PrrC In HeLa cells from a recomblnant vaccinia virus elicited cleavage of intra-cellular tRNALys,3The data justify an inquiry into the possible application of anticodon nuclease as an inhibitor of tRNALys,3-primed HIV replication. They also indicate that the anticodon region of tRNALys is a substrate recognition site and suggest that PrrC harbors the enzymatic activity.",

author = "Nava Shterman and Orna Elroy-stein and Llan Morad and Michal Amitsur and Gabriel Kaufmann",

note = "Funding Information: We thank Niza Frenkel for a suggestion, Dan Canaani, Larry Snyder and Michael Mathews for reading the manuscript, Bernard Moss for the vTF7-3 virus, plasmid pTMl and for reading the manuscript and Stefan Weiss for plasmid ptRNA-Lys,3 and tRNALys>3. NS was supported by fellowships from the Council of Higher Education, Jerusalem, and the Israel Cancer Research Fund. IM was supported by a fellowship from the Levi Eshkol Foundation, Jerusalem. This study was supported by grants from the Israeli Science Foundation and the Israeli Ministry of Arts and Science to GK.",

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doi = "10.1093/nar/23.10.1744",

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T1 - Cleavage of the HIV replication primer tRNALys,3 in human cells expressing bacterial anticodon nuclease

AU - Shterman, Nava

AU - Elroy-stein, Orna

AU - Morad, Llan

AU - Amitsur, Michal

AU - Kaufmann, Gabriel

N1 - Funding Information: We thank Niza Frenkel for a suggestion, Dan Canaani, Larry Snyder and Michael Mathews for reading the manuscript, Bernard Moss for the vTF7-3 virus, plasmid pTMl and for reading the manuscript and Stefan Weiss for plasmid ptRNA-Lys,3 and tRNALys>3. NS was supported by fellowships from the Council of Higher Education, Jerusalem, and the Israel Cancer Research Fund. IM was supported by a fellowship from the Levi Eshkol Foundation, Jerusalem. This study was supported by grants from the Israeli Science Foundation and the Israeli Ministry of Arts and Science to GK.

PY - 1995/5/25

Y1 - 1995/5/25

N2 - Anticodon nuclease is a bacterial restriction enzyme directed against tRNALv8. We report that anticodon nuclease also cleaves mammalian tRNALys molecules, with preference and site specificity shown towards the natural substrate. Expression of the anticodon nuclease core polypeptide PrrC In HeLa cells from a recomblnant vaccinia virus elicited cleavage of intra-cellular tRNALys,3The data justify an inquiry into the possible application of anticodon nuclease as an inhibitor of tRNALys,3-primed HIV replication. They also indicate that the anticodon region of tRNALys is a substrate recognition site and suggest that PrrC harbors the enzymatic activity.

AB - Anticodon nuclease is a bacterial restriction enzyme directed against tRNALv8. We report that anticodon nuclease also cleaves mammalian tRNALys molecules, with preference and site specificity shown towards the natural substrate. Expression of the anticodon nuclease core polypeptide PrrC In HeLa cells from a recomblnant vaccinia virus elicited cleavage of intra-cellular tRNALys,3The data justify an inquiry into the possible application of anticodon nuclease as an inhibitor of tRNALys,3-primed HIV replication. They also indicate that the anticodon region of tRNALys is a substrate recognition site and suggest that PrrC harbors the enzymatic activity.

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M3 - מאמר

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EP - 1749

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 10

ER -

Cleavage of the HIV replication primer tRNA^Lys,3 in human cells expressing bacterial anticodon nuclease

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