Publication

Domain dynamics of the Bacillus subtilis peripheral preprotein translocase subunit SecA

Driessen, A. J. M., 1998, BIOCALORIMETRY. Ladbury, JE. & Chowdhry, BZ. (eds.). CHICHESTER: Wiley, p. 253-265 13 p.

Research output: Chapter in Book/Report/Conference proceedingConference contributionAcademicpeer-review

APA

Driessen, A. J. M. (1998). Domain dynamics of the Bacillus subtilis peripheral preprotein translocase subunit SecA. In JE. Ladbury, & BZ. Chowdhry (Eds.), BIOCALORIMETRY (pp. 253-265). CHICHESTER: Wiley.

Author

Driessen, A.J.M. / Domain dynamics of the Bacillus subtilis peripheral preprotein translocase subunit SecA. BIOCALORIMETRY. editor / JE Ladbury ; BZ Chowdhry. CHICHESTER : Wiley, 1998. pp. 253-265

Harvard

Driessen, AJM 1998, Domain dynamics of the Bacillus subtilis peripheral preprotein translocase subunit SecA. in JE Ladbury & BZ Chowdhry (eds), BIOCALORIMETRY. Wiley, CHICHESTER, pp. 253-265, Conference on the Applications of Calorimetry in the Biological Sciences, 01/09/1996.

Standard

Domain dynamics of the Bacillus subtilis peripheral preprotein translocase subunit SecA. / Driessen, A.J.M.

BIOCALORIMETRY. ed. / JE Ladbury; BZ Chowdhry. CHICHESTER : Wiley, 1998. p. 253-265.

Research output: Chapter in Book/Report/Conference proceedingConference contributionAcademicpeer-review

Vancouver

Driessen AJM. Domain dynamics of the Bacillus subtilis peripheral preprotein translocase subunit SecA. In Ladbury JE, Chowdhry BZ, editors, BIOCALORIMETRY. CHICHESTER: Wiley. 1998. p. 253-265


BibTeX

@inproceedings{5fb2d0e5dd3646c5868c18412ea92b72,
title = "Domain dynamics of the Bacillus subtilis peripheral preprotein translocase subunit SecA",
abstract = "The homodimeric SecA protein is the peripheral subunit of the preprotein translocase in bacteria. It promotes the preprotein translocation across the cytoplasmic membrane by nucleotide-modulated co-insertion and de-insertion into the integral domain of the translocase. SecA has two essential nucleotide binding sites (NBS): the high-affinity NBS-I resides in the amino-terminal domain of the protein and the low-affinity NBS-II is localized at 2/3 of the protein sequence. The nucleotide bound states of soluble SecA were studied by differential scanning calorimetry (DSC). Thermal unfolding reveals that the amino- and carboxy-terminal halves of SecA unfold independently with a transition midpoint of 49 and 40 degrees C, respectively. Binding of ADP to NBS-I increased the interaction between the two domains, whereas binding of AMPPNP does not influence this interaction. When ADP binds both NBS-I and NBS-II, SecA seems to have a more compact globular conformation, whereas binding of AMP-PNP seems to cause a more extended conformation. It is concluded that SecA is a two-domain protein and that the interaction between both domains is modulated by nucleotides. The compact ADP-bound conformation may resemble the membrane-de-inserted state of SecA, while the more extended ATP bound conformation may correspond to the membrane-inserted form of SecA.",
keywords = "DIFFERENTIAL SCANNING CALORIMETRY, DISTINCT ATP-BINDING, ESCHERICHIA-COLI, PROTEIN TRANSLOCATION, MEMBRANE, COMPLEMENTATION, IDENTIFICATION, VECTORS, DRIVEN, INVIVO",
author = "A.J.M. Driessen",
year = "1998",
language = "English",
isbn = "0-471-97781-0",
pages = "253--265",
editor = "JE Ladbury and BZ Chowdhry",
booktitle = "BIOCALORIMETRY",
publisher = "Wiley",

}

RIS

TY - GEN

T1 - Domain dynamics of the Bacillus subtilis peripheral preprotein translocase subunit SecA

AU - Driessen, A.J.M.

PY - 1998

Y1 - 1998

N2 - The homodimeric SecA protein is the peripheral subunit of the preprotein translocase in bacteria. It promotes the preprotein translocation across the cytoplasmic membrane by nucleotide-modulated co-insertion and de-insertion into the integral domain of the translocase. SecA has two essential nucleotide binding sites (NBS): the high-affinity NBS-I resides in the amino-terminal domain of the protein and the low-affinity NBS-II is localized at 2/3 of the protein sequence. The nucleotide bound states of soluble SecA were studied by differential scanning calorimetry (DSC). Thermal unfolding reveals that the amino- and carboxy-terminal halves of SecA unfold independently with a transition midpoint of 49 and 40 degrees C, respectively. Binding of ADP to NBS-I increased the interaction between the two domains, whereas binding of AMPPNP does not influence this interaction. When ADP binds both NBS-I and NBS-II, SecA seems to have a more compact globular conformation, whereas binding of AMP-PNP seems to cause a more extended conformation. It is concluded that SecA is a two-domain protein and that the interaction between both domains is modulated by nucleotides. The compact ADP-bound conformation may resemble the membrane-de-inserted state of SecA, while the more extended ATP bound conformation may correspond to the membrane-inserted form of SecA.

AB - The homodimeric SecA protein is the peripheral subunit of the preprotein translocase in bacteria. It promotes the preprotein translocation across the cytoplasmic membrane by nucleotide-modulated co-insertion and de-insertion into the integral domain of the translocase. SecA has two essential nucleotide binding sites (NBS): the high-affinity NBS-I resides in the amino-terminal domain of the protein and the low-affinity NBS-II is localized at 2/3 of the protein sequence. The nucleotide bound states of soluble SecA were studied by differential scanning calorimetry (DSC). Thermal unfolding reveals that the amino- and carboxy-terminal halves of SecA unfold independently with a transition midpoint of 49 and 40 degrees C, respectively. Binding of ADP to NBS-I increased the interaction between the two domains, whereas binding of AMPPNP does not influence this interaction. When ADP binds both NBS-I and NBS-II, SecA seems to have a more compact globular conformation, whereas binding of AMP-PNP seems to cause a more extended conformation. It is concluded that SecA is a two-domain protein and that the interaction between both domains is modulated by nucleotides. The compact ADP-bound conformation may resemble the membrane-de-inserted state of SecA, while the more extended ATP bound conformation may correspond to the membrane-inserted form of SecA.

KW - DIFFERENTIAL SCANNING CALORIMETRY

KW - DISTINCT ATP-BINDING

KW - ESCHERICHIA-COLI

KW - PROTEIN TRANSLOCATION

KW - MEMBRANE

KW - COMPLEMENTATION

KW - IDENTIFICATION

KW - VECTORS

KW - DRIVEN

KW - INVIVO

M3 - Conference contribution

SN - 0-471-97781-0

SP - 253

EP - 265

BT - BIOCALORIMETRY

A2 - Ladbury, JE

A2 - Chowdhry, BZ

PB - Wiley

CY - CHICHESTER

ER -

ID: 1240434