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The Stable Interaction Between Signal Peptidase LepB of Escherichia coli and Nuclease Bacteriocins Promotes Toxin Entry into the Cytoplasm
- Source :
- Journal of Biological Chemistry, Journal of Biological Chemistry, 2015, 290 (52), pp.30783-30796. ⟨10.1074/jbc.M115.691907⟩, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (52), pp.30783-30796. ⟨10.1074/jbc.M115.691907⟩, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (52), pp.30783-96. 〈10.1074/jbc.M115.691907〉
- Publication Year :
- 2015
- Publisher :
- HAL CCSD, 2015.
-
Abstract
- International audience; LepB is a key membrane component of the cellular secretion machinery, which releases secreted proteins into the periplasm by cleaving the inner membrane-bound leader. We showed that LepB is also an essential component of the machinery hijacked by the tRNase colicin D for its import. Here we demonstrate that this non-catalytic activity of LepB is to promote the association of the central domain of colicin D with the inner membrane before the FtsH-dependent proteolytic processing and translocation of the toxic tRNase domain into the cytoplasm. The novel structural role of LepB results in a stable interaction with colicin D, with a stoichiometry of 1:1 and a nanomolar Kd determined in vitro. LepB provides a chaperone-like function for the penetration of several nuclease-type bacteriocins into target cells. The colicin-LepB interaction is shown to require only a short peptide sequence within the central domain of these bacteriocins and to involve residues present in the short C-terminal Box E of LepB. Genomic screening identified the conserved LepB binding motif in colicin-like ORFs from 13 additional bacterial species. These findings establish a new paradigm for the functional adaptability of an essential inner-membrane enzyme.
- Subjects :
- Cytoplasm
LepB
Amino Acid Motifs
MESH: Escherichia coli Proteins
MESH: Amino Acid Sequence
Biochemistry
endonuclease
MESH: Amino Acid Motifs
MESH: Protein Structure, Tertiary
MESH: Bacteriocins
Bacteriocins
MESH: Serine Endopeptidases
Peptide sequence
membrane
0303 health sciences
Signal peptidase
Deoxyribonucleases
biology
MESH: Escherichia coli
Escherichia coli Proteins
Serine Endopeptidases
Colicin
MESH: Membrane Proteins
colicin
Protein Binding
MESH: Ribonucleases
MESH: Biological Transport
Bacterial Toxins
Molecular Sequence Data
MESH: Sequence Alignment
Sequence alignment
03 medical and health sciences
Ribonucleases
Bacteriocin
bacteriocin
Membrane Biology
[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN]
Escherichia coli
Inner membrane
MESH: Protein Binding
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
Amino Acid Sequence
Molecular Biology
030304 developmental biology
Nuclease
MESH: Molecular Sequence Data
[ SDV ] Life Sciences [q-bio]
030306 microbiology
MESH: Cytoplasm
microbiology
Membrane Proteins
toxicity
Biological Transport
protease
Cell Biology
Periplasmic space
biochemical phenomena, metabolism, and nutrition
Protein Structure, Tertiary
MESH: Bacterial Toxins
biology.protein
bacteria
protein import
Sequence Alignment
MESH: Deoxyribonucleases
Subjects
Details
- Language :
- English
- ISSN :
- 00219258 and 1083351X
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry, Journal of Biological Chemistry, 2015, 290 (52), pp.30783-30796. ⟨10.1074/jbc.M115.691907⟩, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (52), pp.30783-30796. ⟨10.1074/jbc.M115.691907⟩, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (52), pp.30783-96. 〈10.1074/jbc.M115.691907〉
- Accession number :
- edsair.doi.dedup.....f0493d95e57403b1344cc0ad529afed3
- Full Text :
- https://doi.org/10.1074/jbc.M115.691907⟩