Price of disorder in the lac repressor hinge helix

Danielle Seckfort; B. Montgomery Pettitt

doi:10.1002/bip.23239

Price of disorder in the lac repressor hinge helix

Danielle Seckfort, B. Montgomery Pettitt

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

The Lac system of genes has been pivotal in understanding gene regulation. When the lac repressor protein binds to the correct DNA sequence, the hinge region of the protein goes through a disorder to order transition. The structure of this region of the protein is well understood when it is in this bound conformation, but less so when it is not. Structural studies show that this region is flexible. Our simulations show this region is extremely flexible in solution; however, a high concentration of salt can help kinetically trap the hinge helix. Thermodynamically, disorder is more favorable without the DNA present.

Original language	English (US)
Article number	e23239
Journal	Biopolymers
Volume	110
Issue number	1
DOIs	https://doi.org/10.1002/bip.23239
State	Published - Jan 2019

Keywords

LacI
MD simulations
disorder to order transition
disordered proteins
metadynamics
protein
salt stability

ASJC Scopus subject areas

Biophysics
Biochemistry
Biomaterials
Organic Chemistry

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10.1002/bip.23239

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title = "Price of disorder in the lac repressor hinge helix",

abstract = "The Lac system of genes has been pivotal in understanding gene regulation. When the lac repressor protein binds to the correct DNA sequence, the hinge region of the protein goes through a disorder to order transition. The structure of this region of the protein is well understood when it is in this bound conformation, but less so when it is not. Structural studies show that this region is flexible. Our simulations show this region is extremely flexible in solution; however, a high concentration of salt can help kinetically trap the hinge helix. Thermodynamically, disorder is more favorable without the DNA present.",

keywords = "LacI, MD simulations, disorder to order transition, disordered proteins, metadynamics, protein, salt stability",

author = "Danielle Seckfort and {Montgomery Pettitt}, B.",

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AB - The Lac system of genes has been pivotal in understanding gene regulation. When the lac repressor protein binds to the correct DNA sequence, the hinge region of the protein goes through a disorder to order transition. The structure of this region of the protein is well understood when it is in this bound conformation, but less so when it is not. Structural studies show that this region is flexible. Our simulations show this region is extremely flexible in solution; however, a high concentration of salt can help kinetically trap the hinge helix. Thermodynamically, disorder is more favorable without the DNA present.

KW - LacI

KW - MD simulations

KW - disorder to order transition

KW - disordered proteins

KW - metadynamics

KW - protein

KW - salt stability

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Price of disorder in the lac repressor hinge helix

Abstract

Keywords

ASJC Scopus subject areas

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