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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
1997-7-29
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pubmed:abstractText |
Transposition of phage Mu is catalyzed by an extremely stable transposase-DNA complex. Once recombination is complete, the Escherichia coli ClpX protein, a member of the Clp/Hsp100 chaperone family, initiates disassembly of the complex for phage DNA replication to commence. To understand how the transition between recombination and replication is controlled, we investigated how transposase-DNA complexes are recognized by ClpX. We find that a 10-amino-acid peptide from the carboxy-terminal domain of transposase is required for its recognition by ClpX. This short, positively charged peptide is also sufficient to convert a heterologous protein into a ClpX substrate. The region of transposase that interacts with the transposition activator, MuB protein, is also defined further and found to overlap with that recognized by ClpX. As a consequence, MuB inhibits disassembly of several transposase-DNA complexes that are intermediates in recombination. This ability of MuB to block access to transposase suggests a mechanism for restricting ClpX-mediated remodeling to the proper stage during replicative transposition. We propose that overlap of sequences involved in subunit interactions and those that target a protein for remodeling or destruction may be a useful design for proteins that function in pathways where remodeling or degradation must be regulated.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/ClpX protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidase Clp,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/MuB protein, Enterobacteria phage Mu,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transposases,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0890-9369
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1561-72
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pubmed:dateRevised |
2009-9-3
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pubmed:meshHeading |
pubmed-meshheading:9203582-Adenosine Triphosphatases,
pubmed-meshheading:9203582-Amino Acid Sequence,
pubmed-meshheading:9203582-Bacteriophage mu,
pubmed-meshheading:9203582-Binding Sites,
pubmed-meshheading:9203582-DNA Nucleotidyltransferases,
pubmed-meshheading:9203582-DNA-Binding Proteins,
pubmed-meshheading:9203582-Endopeptidase Clp,
pubmed-meshheading:9203582-Escherichia coli,
pubmed-meshheading:9203582-Escherichia coli Proteins,
pubmed-meshheading:9203582-Kinetics,
pubmed-meshheading:9203582-Models, Structural,
pubmed-meshheading:9203582-Molecular Chaperones,
pubmed-meshheading:9203582-Molecular Sequence Data,
pubmed-meshheading:9203582-Mutagenesis, Site-Directed,
pubmed-meshheading:9203582-Polymerase Chain Reaction,
pubmed-meshheading:9203582-Recombinant Proteins,
pubmed-meshheading:9203582-Recombination, Genetic,
pubmed-meshheading:9203582-Transposases,
pubmed-meshheading:9203582-Viral Proteins
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pubmed:year |
1997
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pubmed:articleTitle |
ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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