Inhibition of the p66/p51 form of human immunodeficiency virus reverse transcriptase by tRNA(Lys).
Identifieur interne : 002A28 ( PubMed/Corpus ); précédent : 002A27; suivant : 002A29Inhibition of the p66/p51 form of human immunodeficiency virus reverse transcriptase by tRNA(Lys).
Auteurs : B. Bordier ; L. Tarrago-Litvak ; M L Sallafranque-Andreola ; D. Robert ; D. Tharaud ; M. Fournier ; P J Barr ; S. Litvak ; L. Sarih-CottinSource :
- Nucleic acids research [ 0305-1048 ] ; 1990.
English descriptors
- KwdEn :
- Base Sequence, DNA (biosynthesis), DNA Polymerase II (antagonists & inhibitors), HIV (enzymology), Molecular Sequence Data, RNA, Transfer, Amino Acid-Specific (pharmacology), RNA, Transfer, Lys (pharmacology), RNA, Transfer, Phe (pharmacology), RNA, Transfer, Trp (pharmacology), Recombinant Proteins, Reverse Transcriptase Inhibitors, Ribonuclease T1 (pharmacology), Ribonuclease, Pancreatic (pharmacology).
- MESH :
- chemical , antagonists & inhibitors : DNA Polymerase II.
- chemical , biosynthesis : DNA.
- enzymology : HIV.
- chemical , pharmacology : RNA, Transfer, Amino Acid-Specific, RNA, Transfer, Lys, RNA, Transfer, Phe, RNA, Transfer, Trp, Ribonuclease T1, Ribonuclease, Pancreatic.
- Base Sequence, Molecular Sequence Data, Recombinant Proteins, Reverse Transcriptase Inhibitors.
Abstract
Human immunodeficiency virus (HIV) reverse transcriptase (RT) uses host tRNA(Lys) partially annealed to the primer binding site (PBS) as primer for the initiation of cDNA synthesis. When assaying cDNA synthesis with a template-primer complex formed by an RNA fragment carrying the PBS site and bovine tRNA(Lys) we noticed that an excess of primer tRNA inhibited strongly the DNA polymerase activity of a recombinant HIV RT (p66-p51 heterodimeric form) produced in transformed yeast cells. The same inhibitory effect was observed with animal DNA polymerase alpha, while avian retrovirus RT was neither affected by tRNA(Lys) nor by its specific primer tRNA(Trp). Although the strongest inhibition was observed with tRNA(Lys), other tRNas like tRNA(Phe) and tRNA(Trp) inhibited also the HIV RT, whereas tRNAs specific for valine, proline and glycine had no effect on enzyme activity. Digestion of tRNA(Lys) with pancreatic RNase abolished the inhibition; on the other hand T1 RNase digestion had no effect on the inhibition suggesting a role of the anticodon region in this effect. The 12- and 14-mers corresponding to the anticodon regions of the three bovine tRNA(Lys) isoacceptors inhibited RT activity, indicating that at least an important part of the inhibitory effect could be ascribed to this tRNA region. A strong stimulation of DNA polymerase activity was observed when the effect of tRNA(Lys) was assayed on a recombinant HIV reverse transcriptase produced in a protease deficient yeast strain, which leads to the production of an active p66 enzyme. The same tRNAs that inhibited strongly the heterodimeric form stimulated the p66 form of HIV reverse transcriptase. The results suggest that although both enzymatic forms are able to interact with tRNA(Lys) the topography, as well as the functional implications of the interaction between the precursor and the mature form of HIV reverse transcriptase with the tRNA(Lys) primer, are different.
DOI: 10.1093/nar/18.3.429
PubMed: 1689823
Links to Exploration step
pubmed:1689823Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Inhibition of the p66/p51 form of human immunodeficiency virus reverse transcriptase by tRNA(Lys).</title><author><name sortKey="Bordier, B" sort="Bordier, B" uniqKey="Bordier B" first="B" last="Bordier">B. Bordier</name><affiliation><nlm:affiliation>Institut de Biochimie Cellulaire et Neurochimie du CNRS, Bordeaux, France.</nlm:affiliation></affiliation></author><author><name sortKey="Tarrago Litvak, L" sort="Tarrago Litvak, L" uniqKey="Tarrago Litvak L" first="L" last="Tarrago-Litvak">L. Tarrago-Litvak</name></author><author><name sortKey="Sallafranque Andreola, M L" sort="Sallafranque Andreola, M L" uniqKey="Sallafranque Andreola M" first="M L" last="Sallafranque-Andreola">M L Sallafranque-Andreola</name></author><author><name sortKey="Robert, D" sort="Robert, D" uniqKey="Robert D" first="D" last="Robert">D. Robert</name></author><author><name sortKey="Tharaud, D" sort="Tharaud, D" uniqKey="Tharaud D" first="D" last="Tharaud">D. Tharaud</name></author><author><name sortKey="Fournier, M" sort="Fournier, M" uniqKey="Fournier M" first="M" last="Fournier">M. Fournier</name></author><author><name sortKey="Barr, P J" sort="Barr, P J" uniqKey="Barr P" first="P J" last="Barr">P J Barr</name></author><author><name sortKey="Litvak, S" sort="Litvak, S" uniqKey="Litvak S" first="S" last="Litvak">S. Litvak</name></author><author><name sortKey="Sarih Cottin, L" sort="Sarih Cottin, L" uniqKey="Sarih Cottin L" first="L" last="Sarih-Cottin">L. Sarih-Cottin</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1990">1990</date><idno type="RBID">pubmed:1689823</idno><idno type="pmid">1689823</idno><idno type="doi">10.1093/nar/18.3.429</idno><idno type="wicri:Area/PubMed/Corpus">002A28</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002A28</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Inhibition of the p66/p51 form of human immunodeficiency virus reverse transcriptase by tRNA(Lys).</title><author><name sortKey="Bordier, B" sort="Bordier, B" uniqKey="Bordier B" first="B" last="Bordier">B. Bordier</name><affiliation><nlm:affiliation>Institut de Biochimie Cellulaire et Neurochimie du CNRS, Bordeaux, France.</nlm:affiliation></affiliation></author><author><name sortKey="Tarrago Litvak, L" sort="Tarrago Litvak, L" uniqKey="Tarrago Litvak L" first="L" last="Tarrago-Litvak">L. Tarrago-Litvak</name></author><author><name sortKey="Sallafranque Andreola, M L" sort="Sallafranque Andreola, M L" uniqKey="Sallafranque Andreola M" first="M L" last="Sallafranque-Andreola">M L Sallafranque-Andreola</name></author><author><name sortKey="Robert, D" sort="Robert, D" uniqKey="Robert D" first="D" last="Robert">D. Robert</name></author><author><name sortKey="Tharaud, D" sort="Tharaud, D" uniqKey="Tharaud D" first="D" last="Tharaud">D. Tharaud</name></author><author><name sortKey="Fournier, M" sort="Fournier, M" uniqKey="Fournier M" first="M" last="Fournier">M. Fournier</name></author><author><name sortKey="Barr, P J" sort="Barr, P J" uniqKey="Barr P" first="P J" last="Barr">P J Barr</name></author><author><name sortKey="Litvak, S" sort="Litvak, S" uniqKey="Litvak S" first="S" last="Litvak">S. Litvak</name></author><author><name sortKey="Sarih Cottin, L" sort="Sarih Cottin, L" uniqKey="Sarih Cottin L" first="L" last="Sarih-Cottin">L. Sarih-Cottin</name></author></analytic><series><title level="j">Nucleic acids research</title><idno type="ISSN">0305-1048</idno><imprint><date when="1990" type="published">1990</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Base Sequence</term><term>DNA (biosynthesis)</term><term>DNA Polymerase II (antagonists & inhibitors)</term><term>HIV (enzymology)</term><term>Molecular Sequence Data</term><term>RNA, Transfer, Amino Acid-Specific (pharmacology)</term><term>RNA, Transfer, Lys (pharmacology)</term><term>RNA, Transfer, Phe (pharmacology)</term><term>RNA, Transfer, Trp (pharmacology)</term><term>Recombinant Proteins</term><term>Reverse Transcriptase Inhibitors</term><term>Ribonuclease T1 (pharmacology)</term><term>Ribonuclease, Pancreatic (pharmacology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>DNA Polymerase II</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>DNA</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>HIV</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>RNA, Transfer, Amino Acid-Specific</term><term>RNA, Transfer, Lys</term><term>RNA, Transfer, Phe</term><term>RNA, Transfer, Trp</term><term>Ribonuclease T1</term><term>Ribonuclease, Pancreatic</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term><term>Molecular Sequence Data</term><term>Recombinant Proteins</term><term>Reverse Transcriptase Inhibitors</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Human immunodeficiency virus (HIV) reverse transcriptase (RT) uses host tRNA(Lys) partially annealed to the primer binding site (PBS) as primer for the initiation of cDNA synthesis. When assaying cDNA synthesis with a template-primer complex formed by an RNA fragment carrying the PBS site and bovine tRNA(Lys) we noticed that an excess of primer tRNA inhibited strongly the DNA polymerase activity of a recombinant HIV RT (p66-p51 heterodimeric form) produced in transformed yeast cells. The same inhibitory effect was observed with animal DNA polymerase alpha, while avian retrovirus RT was neither affected by tRNA(Lys) nor by its specific primer tRNA(Trp). Although the strongest inhibition was observed with tRNA(Lys), other tRNas like tRNA(Phe) and tRNA(Trp) inhibited also the HIV RT, whereas tRNAs specific for valine, proline and glycine had no effect on enzyme activity. Digestion of tRNA(Lys) with pancreatic RNase abolished the inhibition; on the other hand T1 RNase digestion had no effect on the inhibition suggesting a role of the anticodon region in this effect. The 12- and 14-mers corresponding to the anticodon regions of the three bovine tRNA(Lys) isoacceptors inhibited RT activity, indicating that at least an important part of the inhibitory effect could be ascribed to this tRNA region. A strong stimulation of DNA polymerase activity was observed when the effect of tRNA(Lys) was assayed on a recombinant HIV reverse transcriptase produced in a protease deficient yeast strain, which leads to the production of an active p66 enzyme. The same tRNAs that inhibited strongly the heterodimeric form stimulated the p66 form of HIV reverse transcriptase. The results suggest that although both enzymatic forms are able to interact with tRNA(Lys) the topography, as well as the functional implications of the interaction between the precursor and the mature form of HIV reverse transcriptase with the tRNA(Lys) primer, are different.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1689823</PMID><DateCompleted><Year>1990</Year><Month>04</Month><Day>03</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0305-1048</ISSN><JournalIssue CitedMedium="Print"><Volume>18</Volume><Issue>3</Issue><PubDate><Year>1990</Year><Month>Feb</Month><Day>11</Day></PubDate></JournalIssue><Title>Nucleic acids research</Title><ISOAbbreviation>Nucleic Acids Res.</ISOAbbreviation></Journal><ArticleTitle>Inhibition of the p66/p51 form of human immunodeficiency virus reverse transcriptase by tRNA(Lys).</ArticleTitle><Pagination><MedlinePgn>429-36</MedlinePgn></Pagination><Abstract><AbstractText>Human immunodeficiency virus (HIV) reverse transcriptase (RT) uses host tRNA(Lys) partially annealed to the primer binding site (PBS) as primer for the initiation of cDNA synthesis. When assaying cDNA synthesis with a template-primer complex formed by an RNA fragment carrying the PBS site and bovine tRNA(Lys) we noticed that an excess of primer tRNA inhibited strongly the DNA polymerase activity of a recombinant HIV RT (p66-p51 heterodimeric form) produced in transformed yeast cells. The same inhibitory effect was observed with animal DNA polymerase alpha, while avian retrovirus RT was neither affected by tRNA(Lys) nor by its specific primer tRNA(Trp). Although the strongest inhibition was observed with tRNA(Lys), other tRNas like tRNA(Phe) and tRNA(Trp) inhibited also the HIV RT, whereas tRNAs specific for valine, proline and glycine had no effect on enzyme activity. Digestion of tRNA(Lys) with pancreatic RNase abolished the inhibition; on the other hand T1 RNase digestion had no effect on the inhibition suggesting a role of the anticodon region in this effect. The 12- and 14-mers corresponding to the anticodon regions of the three bovine tRNA(Lys) isoacceptors inhibited RT activity, indicating that at least an important part of the inhibitory effect could be ascribed to this tRNA region. A strong stimulation of DNA polymerase activity was observed when the effect of tRNA(Lys) was assayed on a recombinant HIV reverse transcriptase produced in a protease deficient yeast strain, which leads to the production of an active p66 enzyme. The same tRNAs that inhibited strongly the heterodimeric form stimulated the p66 form of HIV reverse transcriptase. The results suggest that although both enzymatic forms are able to interact with tRNA(Lys) the topography, as well as the functional implications of the interaction between the precursor and the mature form of HIV reverse transcriptase with the tRNA(Lys) primer, are different.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bordier</LastName><ForeName>B</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Institut de Biochimie Cellulaire et Neurochimie du CNRS, Bordeaux, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tarrago-Litvak</LastName><ForeName>L</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Sallafranque-Andreola</LastName><ForeName>M L</ForeName><Initials>ML</Initials></Author><Author ValidYN="Y"><LastName>Robert</LastName><ForeName>D</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Tharaud</LastName><ForeName>D</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Fournier</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Barr</LastName><ForeName>P J</ForeName><Initials>PJ</Initials></Author><Author ValidYN="Y"><LastName>Litvak</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Sarih-Cottin</LastName><ForeName>L</ForeName><Initials>L</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Nucleic Acids 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