Back to Search
Start Over
DnaJ (Hsp40 Protein) Binding to Folded Substrate Impacts KplE1 Prophage Excision Efficiency
- Source :
- Journal of Biological Chemistry, Journal of Biological Chemistry, 2012, 287 (17), pp.14169-14177. ⟨10.1074/jbc.M111.331462⟩, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2012, 287 (17), pp.14169-14177. ⟨10.1074/jbc.M111.331462⟩, Journal of Biological Chemistry, 2012, 287 (17), pp.14169-14177. ⟨10.1074/jbc.m111.331462⟩, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2012, 287 (17), pp.14169-14177. ⟨10.1074/jbc.m111.331462⟩
- Publication Year :
- 2012
- Publisher :
- HAL CCSD, 2012.
-
Abstract
- International audience; Temperate phages mediate gene transfer and can modify the properties of their host organisms through the acquisition of novel genes, a process called lysogeny. The KplE1 prophage is one of the 10 prophage regions in Escherichia coli K12 MG1655. KplE1 is defective for lysis but fully competent for site-specific recombination. The TorI recombination directionality factor is strictly required for prophage excision from the host genome. We have previously shown that DnaJ promotes KplE1 excision by increasing the affinity of TorI for its site-specific recombination DNA target. Here, we provide evidence of a direct association between TorI and DnaJ using in vitro cross-linking assays and limited proteolysis experiments that show that this interaction allows both proteins to be transiently protected from trypsin digestion. Interestingly, NMR titration experiments showed that binding of DnaJ involves specific regions of the TorI structure. These regions, mainly composed of -helices, are located on a surface opposite the DNA-binding site. Taken together, we propose that DnaJ, without the aid of DnaK/GrpE, is capable of increasing the efficiency of KplE1 excision by causing a conformational stabilization that allows TorI to adopt a more favorable conformation for binding to its specific DNA target.
- Subjects :
- endocrine system
[SDV]Life Sciences [q-bio]
Plasma protein binding
Biochemistry
Models, Biological
Prophase
Microbiology
Mass Spectrometry
Protein Structure, Secondary
Substrate Specificity
Bacteriophage
03 medical and health sciences
chemistry.chemical_compound
Protein structure
Lysogenic cycle
mental disorders
[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology
Escherichia coli
Trypsin
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
Site-specific recombination
Binding site
Molecular Biology
Lysogeny
Prophage
030304 developmental biology
Recombination, Genetic
0303 health sciences
Binding Sites
biology
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM]
030306 microbiology
Circular Dichroism
Escherichia coli Proteins
Cell Biology
HSP40 Heat-Shock Proteins
biology.organism_classification
Cell biology
[SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology
Cross-Linking Reagents
chemistry
Virus Activation
DNA
psychological phenomena and processes
Molecular Chaperones
Protein Binding
Subjects
Details
- Language :
- English
- ISSN :
- 00219258 and 1083351X
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry, Journal of Biological Chemistry, 2012, 287 (17), pp.14169-14177. ⟨10.1074/jbc.M111.331462⟩, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2012, 287 (17), pp.14169-14177. ⟨10.1074/jbc.M111.331462⟩, Journal of Biological Chemistry, 2012, 287 (17), pp.14169-14177. ⟨10.1074/jbc.m111.331462⟩, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2012, 287 (17), pp.14169-14177. ⟨10.1074/jbc.m111.331462⟩
- Accession number :
- edsair.doi.dedup.....8c7c66b3b03cefd1c421fd8f2b0730d7
- Full Text :
- https://doi.org/10.1074/jbc.M111.331462⟩