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Bacteriophage λ N protein inhibits transcription slippage by Escherichia coli RNA polymerase

Transcriptional slippage is a class of error in which ribonucleic acid (RNA) polymerase incorporates nucleotides out of register, with respect to the deoxyribonucleic acid (DNA) template. This phenomenon is involved in gene regulation mechanisms and in the development of diverse diseases. The bacter...

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Autores principales: Parks, Adam R., Court, Carolyn, Lubkowska, Lucyna, Jin, Ding J., Kashlev, Mikhail, Court, Donald L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4027172/
https://www.ncbi.nlm.nih.gov/pubmed/24711367
http://dx.doi.org/10.1093/nar/gku203
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author Parks, Adam R.
Court, Carolyn
Lubkowska, Lucyna
Jin, Ding J.
Kashlev, Mikhail
Court, Donald L.
author_facet Parks, Adam R.
Court, Carolyn
Lubkowska, Lucyna
Jin, Ding J.
Kashlev, Mikhail
Court, Donald L.
author_sort Parks, Adam R.
collection PubMed
description Transcriptional slippage is a class of error in which ribonucleic acid (RNA) polymerase incorporates nucleotides out of register, with respect to the deoxyribonucleic acid (DNA) template. This phenomenon is involved in gene regulation mechanisms and in the development of diverse diseases. The bacteriophage λ N protein reduces transcriptional slippage within actively growing cells and in vitro. N appears to stabilize the RNA/DNA hybrid, particularly at the 5′ end, preventing loss of register between transcript and template. This report provides the first evidence of a protein that directly influences transcriptional slippage, and provides a clue about the molecular mechanism of transcription termination and N-mediated antitermination.
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spelling pubmed-40271722014-05-28 Bacteriophage λ N protein inhibits transcription slippage by Escherichia coli RNA polymerase Parks, Adam R. Court, Carolyn Lubkowska, Lucyna Jin, Ding J. Kashlev, Mikhail Court, Donald L. Nucleic Acids Res Nucleic Acid Enzymes Transcriptional slippage is a class of error in which ribonucleic acid (RNA) polymerase incorporates nucleotides out of register, with respect to the deoxyribonucleic acid (DNA) template. This phenomenon is involved in gene regulation mechanisms and in the development of diverse diseases. The bacteriophage λ N protein reduces transcriptional slippage within actively growing cells and in vitro. N appears to stabilize the RNA/DNA hybrid, particularly at the 5′ end, preventing loss of register between transcript and template. This report provides the first evidence of a protein that directly influences transcriptional slippage, and provides a clue about the molecular mechanism of transcription termination and N-mediated antitermination. Oxford University Press 2014-05-01 2014-03-25 /pmc/articles/PMC4027172/ /pubmed/24711367 http://dx.doi.org/10.1093/nar/gku203 Text en © Published by Oxford University Press on behalf of Nucleic Acids Research 2014. This work is written by (a) US Government employee(s) and is in the public domain in the US.
spellingShingle Nucleic Acid Enzymes
Parks, Adam R.
Court, Carolyn
Lubkowska, Lucyna
Jin, Ding J.
Kashlev, Mikhail
Court, Donald L.
Bacteriophage λ N protein inhibits transcription slippage by Escherichia coli RNA polymerase
title Bacteriophage λ N protein inhibits transcription slippage by Escherichia coli RNA polymerase
title_full Bacteriophage λ N protein inhibits transcription slippage by Escherichia coli RNA polymerase
title_fullStr Bacteriophage λ N protein inhibits transcription slippage by Escherichia coli RNA polymerase
title_full_unstemmed Bacteriophage λ N protein inhibits transcription slippage by Escherichia coli RNA polymerase
title_short Bacteriophage λ N protein inhibits transcription slippage by Escherichia coli RNA polymerase
title_sort bacteriophage λ n protein inhibits transcription slippage by escherichia coli rna polymerase
topic Nucleic Acid Enzymes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4027172/
https://www.ncbi.nlm.nih.gov/pubmed/24711367
http://dx.doi.org/10.1093/nar/gku203
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