TY - JOUR
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.
UR - http://www.scopus.com/inward/record.url?scp=0028999426&partnerID=8YFLogxK
U2 - 10.1093/nar/23.10.1744
DO - 10.1093/nar/23.10.1744
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AN - SCOPUS:0028999426
VL - 23
SP - 1744
EP - 1749
JO - Nucleic Acids Research
JF - Nucleic Acids Research
SN - 0305-1048
IS - 10
ER -
