PMID:9203582
| Citation |
Levchenko, I, Yamauchi, M and Baker, TA (1997) ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway. Genes Dev. 11:1561-72 |
|---|---|
| Abstract |
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. |
| Links | |
| Keywords |
Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Bacteriophage mu/genetics; Bacteriophage mu/physiology; Binding Sites; DNA Nucleotidyltransferases/chemistry; DNA Nucleotidyltransferases/metabolism; DNA-Binding Proteins/metabolism; Endopeptidase Clp; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/virology; Escherichia coli Proteins; Kinetics; Models, Structural; Molecular Chaperones; Molecular Sequence Data; Mutagenesis, Site-Directed; Polymerase Chain Reaction; Recombinant Proteins/metabolism; Recombination, Genetic; Transposases; Viral Proteins/metabolism |
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