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Chromatographic analysis of the aminoacyl-trnas which are required for translation of codons at and around the ribosomal frameshift sites of HIV, HTLV-1, and BLV
An examination of the frameshift signals or proposed signals within published sequences of retroviruses and other genetic elements from higher animals shows that each site utilizes a tRNA which normally contains Wybutoxine (Wye) base or Queuine (Q) base in the anticodon loop. We find experimentally...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Published by Elsevier Inc.
1989
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7131661/ https://www.ncbi.nlm.nih.gov/pubmed/2556852 http://dx.doi.org/10.1016/0042-6822(89)90589-8 |
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author | Hatfield, Dolph Feng, Ya-Xiong Lee, Byeong J. Rein, Alan Levin, Judith G. Oroszlan, Stephen |
author_facet | Hatfield, Dolph Feng, Ya-Xiong Lee, Byeong J. Rein, Alan Levin, Judith G. Oroszlan, Stephen |
author_sort | Hatfield, Dolph |
collection | PubMed |
description | An examination of the frameshift signals or proposed signals within published sequences of retroviruses and other genetic elements from higher animals shows that each site utilizes a tRNA which normally contains Wybutoxine (Wye) base or Queuine (Q) base in the anticodon loop. We find experimentally that most of the Phe-tRNA present in HIV-1 infected cells lacks the highly modified Wye base in its anticodon loop and most of the Asn-tRNA in HTLV-1 and BLV infected cells lacks the highly modified Q base in its anticodon loop. Interestingly, Phe-tRNA translates a UUU codon within the ribosomal frameshift signal in HIV and Asn-tRNA translates a AAC codon within the proposed frameshift signals in HTLV-1 and BLV. Thus, the lack of a highly modified base in the anticodon loop of tRNAs in retroviral infected cells is correlated with the participation of these undermodified tRNAs in the corresponding frameshift event. This suggests that the “shifty” tRNAs proposed by Jacks et al. (Cell 55, 447–458, 1988) to carry out frameshifting may be hypomodified isoacceptors. |
format | Online Article Text |
id | pubmed-7131661 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1989 |
publisher | Published by Elsevier Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71316612020-04-08 Chromatographic analysis of the aminoacyl-trnas which are required for translation of codons at and around the ribosomal frameshift sites of HIV, HTLV-1, and BLV Hatfield, Dolph Feng, Ya-Xiong Lee, Byeong J. Rein, Alan Levin, Judith G. Oroszlan, Stephen Virology Short Communication An examination of the frameshift signals or proposed signals within published sequences of retroviruses and other genetic elements from higher animals shows that each site utilizes a tRNA which normally contains Wybutoxine (Wye) base or Queuine (Q) base in the anticodon loop. We find experimentally that most of the Phe-tRNA present in HIV-1 infected cells lacks the highly modified Wye base in its anticodon loop and most of the Asn-tRNA in HTLV-1 and BLV infected cells lacks the highly modified Q base in its anticodon loop. Interestingly, Phe-tRNA translates a UUU codon within the ribosomal frameshift signal in HIV and Asn-tRNA translates a AAC codon within the proposed frameshift signals in HTLV-1 and BLV. Thus, the lack of a highly modified base in the anticodon loop of tRNAs in retroviral infected cells is correlated with the participation of these undermodified tRNAs in the corresponding frameshift event. This suggests that the “shifty” tRNAs proposed by Jacks et al. (Cell 55, 447–458, 1988) to carry out frameshifting may be hypomodified isoacceptors. Published by Elsevier Inc. 1989-12 2004-01-30 /pmc/articles/PMC7131661/ /pubmed/2556852 http://dx.doi.org/10.1016/0042-6822(89)90589-8 Text en Copyright © 1989 Published by Elsevier Inc. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Short Communication Hatfield, Dolph Feng, Ya-Xiong Lee, Byeong J. Rein, Alan Levin, Judith G. Oroszlan, Stephen Chromatographic analysis of the aminoacyl-trnas which are required for translation of codons at and around the ribosomal frameshift sites of HIV, HTLV-1, and BLV |
title | Chromatographic analysis of the aminoacyl-trnas which are required for translation of codons at and around the ribosomal frameshift sites of HIV, HTLV-1, and BLV |
title_full | Chromatographic analysis of the aminoacyl-trnas which are required for translation of codons at and around the ribosomal frameshift sites of HIV, HTLV-1, and BLV |
title_fullStr | Chromatographic analysis of the aminoacyl-trnas which are required for translation of codons at and around the ribosomal frameshift sites of HIV, HTLV-1, and BLV |
title_full_unstemmed | Chromatographic analysis of the aminoacyl-trnas which are required for translation of codons at and around the ribosomal frameshift sites of HIV, HTLV-1, and BLV |
title_short | Chromatographic analysis of the aminoacyl-trnas which are required for translation of codons at and around the ribosomal frameshift sites of HIV, HTLV-1, and BLV |
title_sort | chromatographic analysis of the aminoacyl-trnas which are required for translation of codons at and around the ribosomal frameshift sites of hiv, htlv-1, and blv |
topic | Short Communication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7131661/ https://www.ncbi.nlm.nih.gov/pubmed/2556852 http://dx.doi.org/10.1016/0042-6822(89)90589-8 |
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