A conserved aromatic residue in the autochaperone domain of the autotransporter Hbp is critical for initiation of outer membrane translocation

Z. Soprova, A. Sauri, J.P. van Ulsen, J.R.H. Tame, T. den Blaauwen, W.S.P. Jong, S. Luirink

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Autotransporters are bacterial virulence factors that share a common mechanism by which they are transported to the cell surface. They consist of an N-terminal passenger domain and a C-terminal β-barrel, which has been implicated in translocation of the passenger across the outer membrane (OM). The mechanism of passenger translocation and folding is still unclear but involves a conserved region at the C terminus of the passenger domain, the so-called autochaperone domain. This domain functions in the stepwise translocation process and in the folding of the passenger domain after translocation. In the autotransporter hemoglobin protease (Hbp), the autochaperone domain consists of the last rung of the β-helix and a capping domain. To examine the role of this region, we have mutated several conserved aromatic residues that are oriented toward the core of the β-helix. We found that non-conservative mutations affected secretion with Trp
LanguageEnglish
Pages38224-38233
Number of pages10
JournalJournal of Biological Chemistry
Volume285
Issue number49
DOIs
Publication statusPublished - 2010

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Hemoglobins
Peptide Hydrolases
Membranes
Virulence Factors
Mutation
Type V Secretion Systems

Cite this

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title = "A conserved aromatic residue in the autochaperone domain of the autotransporter Hbp is critical for initiation of outer membrane translocation",
abstract = "Autotransporters are bacterial virulence factors that share a common mechanism by which they are transported to the cell surface. They consist of an N-terminal passenger domain and a C-terminal β-barrel, which has been implicated in translocation of the passenger across the outer membrane (OM). The mechanism of passenger translocation and folding is still unclear but involves a conserved region at the C terminus of the passenger domain, the so-called autochaperone domain. This domain functions in the stepwise translocation process and in the folding of the passenger domain after translocation. In the autotransporter hemoglobin protease (Hbp), the autochaperone domain consists of the last rung of the β-helix and a capping domain. To examine the role of this region, we have mutated several conserved aromatic residues that are oriented toward the core of the β-helix. We found that non-conservative mutations affected secretion with Trp",
author = "Z. Soprova and A. Sauri and {van Ulsen}, J.P. and J.R.H. Tame and {den Blaauwen}, T. and W.S.P. Jong and S. Luirink",
year = "2010",
doi = "10.1074/jbc.M110.180505",
language = "English",
volume = "285",
pages = "38224--38233",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "49",

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A conserved aromatic residue in the autochaperone domain of the autotransporter Hbp is critical for initiation of outer membrane translocation. / Soprova, Z.; Sauri, A.; van Ulsen, J.P.; Tame, J.R.H.; den Blaauwen, T.; Jong, W.S.P.; Luirink, S.

In: Journal of Biological Chemistry, Vol. 285, No. 49, 2010, p. 38224-38233.

Research output: Contribution to JournalArticleAcademicpeer-review

TY - JOUR

T1 - A conserved aromatic residue in the autochaperone domain of the autotransporter Hbp is critical for initiation of outer membrane translocation

AU - Soprova, Z.

AU - Sauri, A.

AU - van Ulsen, J.P.

AU - Tame, J.R.H.

AU - den Blaauwen, T.

AU - Jong, W.S.P.

AU - Luirink, S.

PY - 2010

Y1 - 2010

N2 - Autotransporters are bacterial virulence factors that share a common mechanism by which they are transported to the cell surface. They consist of an N-terminal passenger domain and a C-terminal β-barrel, which has been implicated in translocation of the passenger across the outer membrane (OM). The mechanism of passenger translocation and folding is still unclear but involves a conserved region at the C terminus of the passenger domain, the so-called autochaperone domain. This domain functions in the stepwise translocation process and in the folding of the passenger domain after translocation. In the autotransporter hemoglobin protease (Hbp), the autochaperone domain consists of the last rung of the β-helix and a capping domain. To examine the role of this region, we have mutated several conserved aromatic residues that are oriented toward the core of the β-helix. We found that non-conservative mutations affected secretion with Trp

AB - Autotransporters are bacterial virulence factors that share a common mechanism by which they are transported to the cell surface. They consist of an N-terminal passenger domain and a C-terminal β-barrel, which has been implicated in translocation of the passenger across the outer membrane (OM). The mechanism of passenger translocation and folding is still unclear but involves a conserved region at the C terminus of the passenger domain, the so-called autochaperone domain. This domain functions in the stepwise translocation process and in the folding of the passenger domain after translocation. In the autotransporter hemoglobin protease (Hbp), the autochaperone domain consists of the last rung of the β-helix and a capping domain. To examine the role of this region, we have mutated several conserved aromatic residues that are oriented toward the core of the β-helix. We found that non-conservative mutations affected secretion with Trp

U2 - 10.1074/jbc.M110.180505

DO - 10.1074/jbc.M110.180505

M3 - Article

VL - 285

SP - 38224

EP - 38233

JO - Journal of Biological Chemistry

T2 - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 49

ER -