Publication

Tight Hydrophobic Contacts with the SecB Chaperone Prevent Folding of Substrate Proteins

Bechtluft, P., Kedrov, A., Slotboom, D-J., Nouwen, N., Tans, S. J. & Driessen, A. J. M., 23-Mar-2010, In : Biochemistry. 49, 11, p. 2380-2388 9 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Bechtluft, P., Kedrov, A., Slotboom, D-J., Nouwen, N., Tans, S. J., & Driessen, A. J. M. (2010). Tight Hydrophobic Contacts with the SecB Chaperone Prevent Folding of Substrate Proteins. Biochemistry, 49(11), 2380-2388. https://doi.org/10.1021/bi902051e

Author

Bechtluft, Philipp ; Kedrov, Alexej ; Slotboom, Dirk-Jan ; Nouwen, Nico ; Tans, Sander J. ; Driessen, Arnold J. M. / Tight Hydrophobic Contacts with the SecB Chaperone Prevent Folding of Substrate Proteins. In: Biochemistry. 2010 ; Vol. 49, No. 11. pp. 2380-2388.

Harvard

Bechtluft, P, Kedrov, A, Slotboom, D-J, Nouwen, N, Tans, SJ & Driessen, AJM 2010, 'Tight Hydrophobic Contacts with the SecB Chaperone Prevent Folding of Substrate Proteins', Biochemistry, vol. 49, no. 11, pp. 2380-2388. https://doi.org/10.1021/bi902051e

Standard

Tight Hydrophobic Contacts with the SecB Chaperone Prevent Folding of Substrate Proteins. / Bechtluft, Philipp; Kedrov, Alexej; Slotboom, Dirk-Jan; Nouwen, Nico; Tans, Sander J.; Driessen, Arnold J. M.

In: Biochemistry, Vol. 49, No. 11, 23.03.2010, p. 2380-2388.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Bechtluft P, Kedrov A, Slotboom D-J, Nouwen N, Tans SJ, Driessen AJM. Tight Hydrophobic Contacts with the SecB Chaperone Prevent Folding of Substrate Proteins. Biochemistry. 2010 Mar 23;49(11):2380-2388. https://doi.org/10.1021/bi902051e


BibTeX

@article{9ce630d449b24fdf9c8d33cfa7248c87,
title = "Tight Hydrophobic Contacts with the SecB Chaperone Prevent Folding of Substrate Proteins",
abstract = "The molecular chaperone SecB binds to hydrophobic sections of unfolded secretory proteins and thereby prevents their premature folding prior to secretion by the translocase of Escherichia coli. Here, we have Investigated the effect of the single-residue mutation of leucine 42 to arginine (L42R) centrally positioned in the polypeptide binding pocket of SecB on its chaperonin function. The mutant retains its tetrameric structure and SecA targeting function but is defective in its holdase activity. Isothermal titration calorimetry and single-molecule optical tweezer studies suggest that the SecB(L42R) mutant exhibits a reduced polypeptide binding affinity allowing for partial folding of the bound polypeptide chain rendering it translocation-incompetent.",
keywords = "MALTOSE-BINDING PROTEIN, ESCHERICHIA-COLI, TERTIARY STRUCTURE, CRYSTAL-STRUCTURE, LIGHT-SCATTERING, TRANSLOCATION, EXPORT, MEMBRANE, EQUILIBRIUM, RECOGNITION",
author = "Philipp Bechtluft and Alexej Kedrov and Dirk-Jan Slotboom and Nico Nouwen and Tans, {Sander J.} and Driessen, {Arnold J. M.}",
year = "2010",
month = mar,
day = "23",
doi = "10.1021/bi902051e",
language = "English",
volume = "49",
pages = "2380--2388",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "AMER CHEMICAL SOC",
number = "11",

}

RIS

TY - JOUR

T1 - Tight Hydrophobic Contacts with the SecB Chaperone Prevent Folding of Substrate Proteins

AU - Bechtluft, Philipp

AU - Kedrov, Alexej

AU - Slotboom, Dirk-Jan

AU - Nouwen, Nico

AU - Tans, Sander J.

AU - Driessen, Arnold J. M.

PY - 2010/3/23

Y1 - 2010/3/23

N2 - The molecular chaperone SecB binds to hydrophobic sections of unfolded secretory proteins and thereby prevents their premature folding prior to secretion by the translocase of Escherichia coli. Here, we have Investigated the effect of the single-residue mutation of leucine 42 to arginine (L42R) centrally positioned in the polypeptide binding pocket of SecB on its chaperonin function. The mutant retains its tetrameric structure and SecA targeting function but is defective in its holdase activity. Isothermal titration calorimetry and single-molecule optical tweezer studies suggest that the SecB(L42R) mutant exhibits a reduced polypeptide binding affinity allowing for partial folding of the bound polypeptide chain rendering it translocation-incompetent.

AB - The molecular chaperone SecB binds to hydrophobic sections of unfolded secretory proteins and thereby prevents their premature folding prior to secretion by the translocase of Escherichia coli. Here, we have Investigated the effect of the single-residue mutation of leucine 42 to arginine (L42R) centrally positioned in the polypeptide binding pocket of SecB on its chaperonin function. The mutant retains its tetrameric structure and SecA targeting function but is defective in its holdase activity. Isothermal titration calorimetry and single-molecule optical tweezer studies suggest that the SecB(L42R) mutant exhibits a reduced polypeptide binding affinity allowing for partial folding of the bound polypeptide chain rendering it translocation-incompetent.

KW - MALTOSE-BINDING PROTEIN

KW - ESCHERICHIA-COLI

KW - TERTIARY STRUCTURE

KW - CRYSTAL-STRUCTURE

KW - LIGHT-SCATTERING

KW - TRANSLOCATION

KW - EXPORT

KW - MEMBRANE

KW - EQUILIBRIUM

KW - RECOGNITION

U2 - 10.1021/bi902051e

DO - 10.1021/bi902051e

M3 - Article

VL - 49

SP - 2380

EP - 2388

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 11

ER -

ID: 5047847