Tn7 recognizes transposition target structures associated with DNA replication using the DNA-binding protein TnsE

We report that the bacterial transposon Tn7 selects targets by recognizing features associated with DNA replication using the transposon-encoded DNA-binding protein TnsE. We show that Tn7 transposition directed by TnsE occurs in one orientation with respect to chromosomal DNA replication, indicating...

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Main Authors: Peters, Joseph E., Craig, Nancy L.
Formato: Artigo
Idioma:en
Publicado em: Cold Spring Harbor Laboratory Press 2001
Assuntos:
Research Paper
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC312648/
https://ncbi.nlm.nih.gov/pubmed/11274058
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1101/gad.870201
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spelling pubmed-3126482004-11-08 Tn7 recognizes transposition target structures associated with DNA replication using the DNA-binding protein TnsE Peters, Joseph E. Craig, Nancy L. Genes Dev Research Paper We report that the bacterial transposon Tn7 selects targets by recognizing features associated with DNA replication using the transposon-encoded DNA-binding protein TnsE. We show that Tn7 transposition directed by TnsE occurs in one orientation with respect to chromosomal DNA replication, indicating that a structure or complex involved in DNA replication is likely to be a critical determinant of TnsE insertion. We find that mutant TnsE proteins that allow higher levels of transposition also bind DNA better than the wild-type protein. The increased binding affinity displayed by the TnsE high-activity mutants indicates that DNA binding is relevant to transposition activity and suggests that TnsE interacts directly with target DNAs. In vitro, TnsE interacts preferentially with certain DNA structures, indicating a mechanism for the TnsE-mediated orientation and insertion preference. The pattern of TnsE-mediated insertion events around the Escherichia coli chromosome provides insight into how DNA replication forks proceed in vivo. Cold Spring Harbor Laboratory Press 2001-03-15 /pmc/articles/PMC312648/ /pubmed/11274058 http://dx.doi.org/10.1101/gad.870201 Text en Copyright © 2001, Cold Spring Harbor Laboratory Press
institution US National Library of Medicine
collection PubMed Central
language en
format Article
topic Research Paper
spellingShingle Research Paper
Peters, Joseph E.
Craig, Nancy L.
Tn7 recognizes transposition target structures associated with DNA replication using the DNA-binding protein TnsE
description We report that the bacterial transposon Tn7 selects targets by recognizing features associated with DNA replication using the transposon-encoded DNA-binding protein TnsE. We show that Tn7 transposition directed by TnsE occurs in one orientation with respect to chromosomal DNA replication, indicating that a structure or complex involved in DNA replication is likely to be a critical determinant of TnsE insertion. We find that mutant TnsE proteins that allow higher levels of transposition also bind DNA better than the wild-type protein. The increased binding affinity displayed by the TnsE high-activity mutants indicates that DNA binding is relevant to transposition activity and suggests that TnsE interacts directly with target DNAs. In vitro, TnsE interacts preferentially with certain DNA structures, indicating a mechanism for the TnsE-mediated orientation and insertion preference. The pattern of TnsE-mediated insertion events around the Escherichia coli chromosome provides insight into how DNA replication forks proceed in vivo.
author Peters, Joseph E.
Craig, Nancy L.
author_facet Peters, Joseph E.
Craig, Nancy L.
author_sort Peters, Joseph E.
title Tn7 recognizes transposition target structures associated with DNA replication using the DNA-binding protein TnsE
title_short Tn7 recognizes transposition target structures associated with DNA replication using the DNA-binding protein TnsE
title_full Tn7 recognizes transposition target structures associated with DNA replication using the DNA-binding protein TnsE
title_fullStr Tn7 recognizes transposition target structures associated with DNA replication using the DNA-binding protein TnsE
title_full_unstemmed Tn7 recognizes transposition target structures associated with DNA replication using the DNA-binding protein TnsE
title_sort tn7 recognizes transposition target structures associated with dna replication using the dna-binding protein tnse
publisher Cold Spring Harbor Laboratory Press
publisher_facet Cold Spring Harbor Laboratory Press
publishDate 2001
url https://ncbi.nlm.nih.gov/pmc/articles/PMC312648/
https://ncbi.nlm.nih.gov/pubmed/11274058
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1101/gad.870201
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