Structure and DNA-binding traits of the transition state regulator AbrB.

Olson, Andrew L

Tucker, Ashley T

Bobay, Benjamin G

Soderblom, Erik J

Moseley, M Arthur

Thompson, Richele J

Cavanagh, John

2023-09-01T14:12:18Z

2023-09-01T14:12:18Z

2014-11

2023-09-01T14:12:18Z

The AbrB protein from Bacillus subtilis is a DNA-binding global regulator controlling the onset of a vast array of protective functions under stressful conditions. Such functions include biofilm formation, antibiotic production, competence development, extracellular enzyme production, motility, and sporulation. AbrB orthologs are known in a variety of prokaryotic organisms, most notably in all infectious strains of Clostridia, Listeria, and Bacilli. Despite its central role in bacterial response and defense, its structure has been elusive because of its highly dynamic character. Orienting its N- and C-terminal domains with respect to one another has been especially problematic. Here, we have generated a structure of full-length, tetrameric AbrB using nuclear magnetic resonance, chemical crosslinking, and mass spectrometry. We note that AbrB possesses a strip of positive electrostatic potential encompassing its DNA-binding region and that its C-terminal domain aids in DNA binding.

S0969-2126(14)00282-2

0969-2126

1878-4186

https://hdl.handle.net/10161/28903

eng

Elsevier BV

Structure (London, England : 1993)

10.1016/j.str.2014.08.018

Bacillus subtilis

Bacterial Proteins

DNA-Binding Proteins

Transcription Factors

DNA, Bacterial

Magnetic Resonance Spectroscopy

Binding Sites

Protein Structure, Secondary

Mass Spectrometry

Protein Multimerization

Molecular Docking Simulation

Structure and DNA-binding traits of the transition state regulator AbrB.

Journal article

Bobay, Benjamin G|0000-0003-4775-3686

1650

1656

11

Duke

School of Medicine

Basic Science Departments

Clinical Science Departments

Cell Biology

Medicine

Radiology

Duke Center for Applied Genomics and Precision Medicine

Published

22