Comparing system-specific chaperone interactions with their Tat dependent redox enzyme substrates
Redox enzyme substrates of the twin-arginine translocation (Tat) system contain a RR-motif in their leader peptide and require the assistance of chaperones, redox enzyme maturation proteins (REMPs). Here various regions of the RR-containing oxidoreductase subunit (leader peptide, full preprotein wit...
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Published in | FEBS letters Vol. 584; no. 22; pp. 4553 - 4558 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier B.V
19.11.2010
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Subjects | |
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Abstract | Redox enzyme substrates of the twin-arginine translocation (Tat) system contain a RR-motif in their leader peptide and require the assistance of chaperones, redox enzyme maturation proteins (REMPs). Here various regions of the RR-containing oxidoreductase subunit (leader peptide, full preprotein with and without a leader cleavage site, mature protein) were assayed for interaction with their REMPs. All REMPs bound their preprotein substrates independent of the cleavage site. Some showed binding to either the leader or mature region, whereas in one case only the preprotein bound its REMP. The absence of Tat also influenced the amount of chaperone–substrate interaction.
MINT-
8047497:
FdhE (uniprotkb:
P13024) and
FdoG (uniprotkb:
P32176)
physically interact (MI:
0915) by
two hybrid (MI:
0018)
MINT-
8046441:
HybO (uniprotkb:
P69741) and
HybE (uniprotkb:
P0AAN1)
physically interact (MI:
0915) by
two hybrid (MI:
0018)
MINT-
8046375:
DmsA (uniprotkb:
P18775) and
DmsD (uniprotkb:
P69853)
physically interact (MI:
0915) by
two hybrid (MI:
0018)
MINT-
8046425:
TorA (uniprotkb:
P33225) and
TorD (uniprotkb:
P36662)
physically interact (MI:
0915) by
two hybrid (MI:
0018)
MINT-
8046393:
NarJ (uniprotkb:
P0AF26) and
NarG (uniprotkb:
P09152)
physically interact (MI:
0915) by
two hybrid (MI:
0018)
MINT-
8046409:
NapD (uniprotkb:
P0A9I5) and
NapA (uniprotkb:
P33937)
physically interact (MI:
0915) by
two hybrid (MI:
0018) |
---|---|
AbstractList | Redox enzyme substrates of the twin-arginine translocation (Tat) system contain a RR-motif in their leader peptide and require the assistance of chaperones, redox enzyme maturation proteins (REMPs). Here various regions of the RR-containing oxidoreductase subunit (leader peptide, full preprotein with and without a leader cleavage site, mature protein) were assayed for interaction with their REMPs. All REMPs bound their preprotein substrates independent of the cleavage site. Some showed binding to either the leader or mature region, whereas in one case only the preprotein bound its REMP. The absence of Tat also influenced the amount of chaperone-substrate interaction. MINT‐8046409: NapD (uniprotkb:P0A9I5) and NapA (uniprotkb:P33937) physically interact (MI:0915) by two hybrid (MI:0018) Redox enzyme substrates of the twin-arginine translocation (Tat) system contain a RR-motif in their leader peptide and require the assistance of chaperones, redox enzyme maturation proteins (REMPs). Here various regions of the RR-containing oxidoreductase subunit (leader peptide, full preprotein with and without a leader cleavage site, mature protein) were assayed for interaction with their REMPs. All REMPs bound their preprotein substrates independent of the cleavage site. Some showed binding to either the leader or mature region, whereas in one case only the preprotein bound its REMP. The absence of Tat also influenced the amount of chaperone–substrate interaction. MINT- 8047497: FdhE (uniprotkb: P13024) and FdoG (uniprotkb: P32176) physically interact (MI: 0915) by two hybrid (MI: 0018) MINT- 8046441: HybO (uniprotkb: P69741) and HybE (uniprotkb: P0AAN1) physically interact (MI: 0915) by two hybrid (MI: 0018) MINT- 8046375: DmsA (uniprotkb: P18775) and DmsD (uniprotkb: P69853) physically interact (MI: 0915) by two hybrid (MI: 0018) MINT- 8046425: TorA (uniprotkb: P33225) and TorD (uniprotkb: P36662) physically interact (MI: 0915) by two hybrid (MI: 0018) MINT- 8046393: NarJ (uniprotkb: P0AF26) and NarG (uniprotkb: P09152) physically interact (MI: 0915) by two hybrid (MI: 0018) MINT- 8046409: NapD (uniprotkb: P0A9I5) and NapA (uniprotkb: P33937) physically interact (MI: 0915) by two hybrid (MI: 0018) MINT‐8046409: NapD (uniprotkb:P0A9I5) and NapA (uniprotkb:P33937) physically interact (MI:0915) by two hybrid (MI:0018) |
Author | Chang, Limei Winstone, Tara M.L. Turner, Raymond J. Chan, Catherine S. |
Author_xml | – sequence: 1 givenname: Catherine S. surname: Chan fullname: Chan, Catherine S. – sequence: 2 givenname: Limei surname: Chang fullname: Chang, Limei – sequence: 3 givenname: Tara M.L. surname: Winstone fullname: Winstone, Tara M.L. – sequence: 4 givenname: Raymond J. surname: Turner fullname: Turner, Raymond J. email: turnerr@ucalgary.ca |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20974141$$D View this record in MEDLINE/PubMed |
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CitedBy_id | crossref_primary_10_1021_bi500891d crossref_primary_10_1093_femsre_fuv043 crossref_primary_10_1186_1471_2091_14_28 crossref_primary_10_1371_journal_pone_0201935 crossref_primary_10_1016_j_bbrc_2015_08_079 crossref_primary_10_1016_j_bbamem_2014_08_020 crossref_primary_10_1021_bi4009374 crossref_primary_10_1371_journal_pone_0256715 crossref_primary_10_1016_j_bbamem_2016_01_025 crossref_primary_10_1371_journal_pone_0034159 crossref_primary_10_1074_jbc_M110_213306 crossref_primary_10_1016_j_ijbiomac_2024_129620 crossref_primary_10_3390_molecules28207195 crossref_primary_10_1111_febs_12592 |
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Copyright | 2010 Federation of European Biochemical Societies FEBS Letters 584 (2010) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
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Keywords | REMP Leader sequence System specific chaperone Bacterial two-hybrid Tat BACTH Twin-arginine translocase system Twin arginine translocase Protein maturation |
Language | English |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 These authors contribute equally to the first authorship. Present address: Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of British Columbia, Vancouver, British Columbia, Canada. |
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Snippet | Redox enzyme substrates of the twin-arginine translocation (Tat) system contain a RR-motif in their leader peptide and require the assistance of chaperones,... MINT‐8046409: NapD (uniprotkb:P0A9I5) and NapA (uniprotkb:P33937) physically interact (MI:0915) by two hybrid (MI:0018) MINT‐8046409: NapD (uniprotkb:P0A9I5) and NapA (uniprotkb:P33937) physically interact (MI:0915) by two hybrid (MI:0018) |
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SubjectTerms | Amino Acid Motifs Arginine Bacterial two-hybrid BACTH Catalytic Domain Escherichia coli - enzymology Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Leader sequence Membrane Transport Proteins - chemistry Membrane Transport Proteins - metabolism Molecular Chaperones - metabolism Oxidoreductases - chemistry Oxidoreductases - metabolism Protein Binding Protein maturation Protein Subunits - chemistry Protein Subunits - metabolism redox enzyme maturation protein REMP Substrate Specificity System specific chaperone Tat Twin arginine translocase Twin-arginine translocase system |
Title | Comparing system-specific chaperone interactions with their Tat dependent redox enzyme substrates |
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