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C-terminal amino acid residues of the trimeric autotransporter adhesin YadA of Yersinia enterocolitica are decisive for its recognition and assembly by BamA

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C-terminal amino acid residues of the trimeric autotransporter adhesin YadA of Yersinia enterocolitica are decisive for its recognition and assembly by BamA. / Lehr, U.; Schuetz, M.; Oberhettinger, P.; Ruiz-Perez, F.; Donald, J. W.; Palmer, T.; Linke, D.; Henderson, I. R.; Autenrieth, I. B.

In: Molecular Microbiology, Vol. 78, No. 4, 2010, p. 932-946.

Research output: Contribution to journalArticle

Harvard

Lehr, U, Schuetz, M, Oberhettinger, P, Ruiz-Perez, F, Donald, JW, Palmer, T, Linke, D, Henderson, IR & Autenrieth, IB 2010, 'C-terminal amino acid residues of the trimeric autotransporter adhesin YadA of Yersinia enterocolitica are decisive for its recognition and assembly by BamA' Molecular Microbiology, vol 78, no. 4, pp. 932-946.

APA

Lehr, U., Schuetz, M., Oberhettinger, P., Ruiz-Perez, F., Donald, J. W., Palmer, T., Linke, D., Henderson, I. R., & Autenrieth, I. B. (2010). C-terminal amino acid residues of the trimeric autotransporter adhesin YadA of Yersinia enterocolitica are decisive for its recognition and assembly by BamA. Molecular Microbiology, 78(4), 932-946doi: 10.1111/j.1365-2958.2010.07377.x

Vancouver

Lehr U, Schuetz M, Oberhettinger P, Ruiz-Perez F, Donald JW, Palmer T et al. C-terminal amino acid residues of the trimeric autotransporter adhesin YadA of Yersinia enterocolitica are decisive for its recognition and assembly by BamA. Molecular Microbiology. 2010;78(4):932-946.

Author

Lehr, U.; Schuetz, M.; Oberhettinger, P.; Ruiz-Perez, F.; Donald, J. W.; Palmer, T.; Linke, D.; Henderson, I. R.; Autenrieth, I. B. / C-terminal amino acid residues of the trimeric autotransporter adhesin YadA of Yersinia enterocolitica are decisive for its recognition and assembly by BamA.

In: Molecular Microbiology, Vol. 78, No. 4, 2010, p. 932-946.

Research output: Contribution to journalArticle

Bibtex - Download

@article{d7c7371ee9c44bfebf790147edc5bb53,
title = "C-terminal amino acid residues of the trimeric autotransporter adhesin YadA of Yersinia enterocolitica are decisive for its recognition and assembly by BamA",
author = "U. Lehr and M. Schuetz and P. Oberhettinger and F. Ruiz-Perez and Donald, {J. W.} and T. Palmer and D. Linke and Henderson, {I. R.} and Autenrieth, {I. B.}",
year = "2010",
volume = "78",
number = "4",
pages = "932--946",
journal = "Molecular Microbiology",
issn = "0950-382x",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - C-terminal amino acid residues of the trimeric autotransporter adhesin YadA of Yersinia enterocolitica are decisive for its recognition and assembly by BamA

A1 - Lehr,U.

A1 - Schuetz,M.

A1 - Oberhettinger,P.

A1 - Ruiz-Perez,F.

A1 - Donald,J. W.

A1 - Palmer,T.

A1 - Linke,D.

A1 - Henderson,I. R.

A1 - Autenrieth,I. B.

AU - Lehr,U.

AU - Schuetz,M.

AU - Oberhettinger,P.

AU - Ruiz-Perez,F.

AU - Donald,J. W.

AU - Palmer,T.

AU - Linke,D.

AU - Henderson,I. R.

AU - Autenrieth,I. B.

PY - 2010

Y1 - 2010

N2 - <p>P&gt;The Bam complex is a highly conserved multiprotein machine essential for the assembly of beta-barrel outer membrane proteins. It is composed of the essential outer membrane protein BamA and four outer membrane associated lipoproteins BamB-E. The Yersinia enterocolitica Adhesin A (YadA) is the prototype of trimeric auotransporter adhesins (TAAs), consisting of a head, stalk and a beta-barrel membrane anchor. To investigate the role of BamA in biogenesis of TAAs, we expressed YadA in a BamA-depleted strain of Escherichia coli, which resulted in degradation of YadA. Yeast-two-hybrid experiments and immunofluorescence studies revealed that BamA and YadA interact directly and colocalize. As BamA recognizes the C-terminus of OMPs, we exchanged the nine most C-terminal amino acids of YadA. Substitution of the amino acids in position 1, 3 or 5 from the C-terminus with glycine resulted in DegP-dependent degradation of YadA. Despite degradation all YadA proteins assembled in the outer membrane. In summary we demonstrate that (i) BamA is essential for biogenesis of the TAA YadA, (ii) BamA interacts directly with YadA, (iii) the C-terminal amino acid motif of YadA is important for the BamA-dependent assembly and differs slightly compared with other OMPs, and (iv) BamA and YadA colocalize.</p>

AB - <p>P&gt;The Bam complex is a highly conserved multiprotein machine essential for the assembly of beta-barrel outer membrane proteins. It is composed of the essential outer membrane protein BamA and four outer membrane associated lipoproteins BamB-E. The Yersinia enterocolitica Adhesin A (YadA) is the prototype of trimeric auotransporter adhesins (TAAs), consisting of a head, stalk and a beta-barrel membrane anchor. To investigate the role of BamA in biogenesis of TAAs, we expressed YadA in a BamA-depleted strain of Escherichia coli, which resulted in degradation of YadA. Yeast-two-hybrid experiments and immunofluorescence studies revealed that BamA and YadA interact directly and colocalize. As BamA recognizes the C-terminus of OMPs, we exchanged the nine most C-terminal amino acids of YadA. Substitution of the amino acids in position 1, 3 or 5 from the C-terminus with glycine resulted in DegP-dependent degradation of YadA. Despite degradation all YadA proteins assembled in the outer membrane. In summary we demonstrate that (i) BamA is essential for biogenesis of the TAA YadA, (ii) BamA interacts directly with YadA, (iii) the C-terminal amino acid motif of YadA is important for the BamA-dependent assembly and differs slightly compared with other OMPs, and (iv) BamA and YadA colocalize.</p>

KW - OUTER-MEMBRANE-PROTEIN

KW - CONSERVED BACTERIAL PROTEIN

KW - ESCHERICHIA-COLI

KW - VIRULENCE PLASMID

KW - BINDING DOMAIN

KW - OMP85

KW - SECRETION

KW - PATHWAY

KW - TRANSLOCATION

KW - TRANSPORT

U2 - 10.1111/j.1365-2958.2010.07377.x

DO - 10.1111/j.1365-2958.2010.07377.x

M1 - Article

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382x

IS - 4

VL - 78

SP - 932

EP - 946

ER -

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