Ultrafast structural dynamics of BlsA, a photoreceptor from the pathogenic bacterium Acinetobacter baumannii

Richard Brust; Allison Haigney; Andras Lukacs; Agnieszka Gil; Shahrier Hossain; Kiri Addison; Cheng-Tsung Lai; Michael Towrie; Gregory M. Greetham; Ian P. Clark; Boris Illarionov; Adelbert Bacher; Ryu-Ryun Kim; Markus Fischer; Carlos Simmerling; Stephen R. Meech; Peter J. Tonge

doi:10.1021/jz4023738

Ultrafast structural dynamics of BlsA, a photoreceptor from the pathogenic bacterium Acinetobacter baumannii

Richard Brust, Allison Haigney, Andras Lukacs, Agnieszka Gil, Shahrier Hossain, Kiri Addison, Cheng-Tsung Lai, Michael Towrie, Gregory M. Greetham, Ian P. Clark, Boris Illarionov, Adelbert Bacher, Ryu-Ryun Kim, Markus Fischer, Carlos Simmerling, Stephen R. Meech, Peter J. Tonge

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Abstract

Acinetobacter baumannii is an important human pathogen that can form biofilms and persist under harsh environmental conditions. Biofilm formation and virulence are modulated by blue light, which is thought to be regulated by a BLUF protein, BlsA. To understand the molecular mechanism of light sensing, we have used steady-state and ultrafast vibrational spectroscopy to compare the photoactivation mechanism of BlsA to the BLUF photosensor AppA from Rhodobacter sphaeroides. Although similar photocycles are observed, vibrational data together with homology modeling identify significant differences in the β5 strand in BlsA caused by photoactivation, which are proposed to be directly linked to downstream signaling.

Original language	English
Pages (from-to)	220-224
Number of pages	5
Journal	The Journal of Physical Chemistry Letters
Volume	5
Issue number	1
DOIs	https://doi.org/10.1021/jz4023738
Publication status	Published - 2 Jan 2014

Keywords

blue light using FAD
BLUF domain
BlsA
photosensor
Acinetobacter baumannii
ultrafast time-resolved infrared
AppA

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10.1021/jz4023738Licence: CC BY

Brust_etal_2014_JPhysChemLett
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Final published version, 1.08 MBLicence: CC BY

International Collaboration in Chemistry: BLUF Domain blue light photosensors a paradigm for optogenetics
Meech, S.
Engineering and Physical Sciences Research Council
18/03/13 → 17/03/16
Project: Research

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Brust, R., Haigney, A., Lukacs, A., Gil, A., Hossain, S., Addison, K., Lai, C.-T., Towrie, M., Greetham, G. M., Clark, I. P., Illarionov, B., Bacher, A., Kim, R.-R., Fischer, M., Simmerling, C., Meech, S. R., & Tonge, P. J. (2014). Ultrafast structural dynamics of BlsA, a photoreceptor from the pathogenic bacterium Acinetobacter baumannii. The Journal of Physical Chemistry Letters, 5(1), 220-224. https://doi.org/10.1021/jz4023738

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title = "Ultrafast structural dynamics of BlsA, a photoreceptor from the pathogenic bacterium Acinetobacter baumannii",

abstract = "Acinetobacter baumannii is an important human pathogen that can form biofilms and persist under harsh environmental conditions. Biofilm formation and virulence are modulated by blue light, which is thought to be regulated by a BLUF protein, BlsA. To understand the molecular mechanism of light sensing, we have used steady-state and ultrafast vibrational spectroscopy to compare the photoactivation mechanism of BlsA to the BLUF photosensor AppA from Rhodobacter sphaeroides. Although similar photocycles are observed, vibrational data together with homology modeling identify significant differences in the β5 strand in BlsA caused by photoactivation, which are proposed to be directly linked to downstream signaling.",

keywords = "blue light using FAD, BLUF domain, BlsA, photosensor, Acinetobacter baumannii, ultrafast time-resolved infrared, AppA",

author = "Richard Brust and Allison Haigney and Andras Lukacs and Agnieszka Gil and Shahrier Hossain and Kiri Addison and Cheng-Tsung Lai and Michael Towrie and Greetham, {Gregory M.} and Clark, {Ian P.} and Boris Illarionov and Adelbert Bacher and Ryu-Ryun Kim and Markus Fischer and Carlos Simmerling and Meech, {Stephen R.} and Tonge, {Peter J.}",

year = "2014",

month = jan,

day = "2",

doi = "10.1021/jz4023738",

language = "English",

volume = "5",

pages = "220--224",

journal = "The Journal of Physical Chemistry Letters",

issn = "1948-7185",

publisher = "American Chemical Society",

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Brust, R, Haigney, A, Lukacs, A, Gil, A, Hossain, S, Addison, K, Lai, C-T, Towrie, M, Greetham, GM, Clark, IP, Illarionov, B, Bacher, A, Kim, R-R, Fischer, M, Simmerling, C, Meech, SR & Tonge, PJ 2014, 'Ultrafast structural dynamics of BlsA, a photoreceptor from the pathogenic bacterium Acinetobacter baumannii', The Journal of Physical Chemistry Letters, vol. 5, no. 1, pp. 220-224. https://doi.org/10.1021/jz4023738

TY - JOUR

T1 - Ultrafast structural dynamics of BlsA, a photoreceptor from the pathogenic bacterium Acinetobacter baumannii

AU - Brust, Richard

AU - Haigney, Allison

AU - Lukacs, Andras

AU - Gil, Agnieszka

AU - Hossain, Shahrier

AU - Addison, Kiri

AU - Lai, Cheng-Tsung

AU - Towrie, Michael

AU - Greetham, Gregory M.

AU - Clark, Ian P.

AU - Illarionov, Boris

AU - Bacher, Adelbert

AU - Kim, Ryu-Ryun

AU - Fischer, Markus

AU - Simmerling, Carlos

AU - Meech, Stephen R.

AU - Tonge, Peter J.

PY - 2014/1/2

Y1 - 2014/1/2

N2 - Acinetobacter baumannii is an important human pathogen that can form biofilms and persist under harsh environmental conditions. Biofilm formation and virulence are modulated by blue light, which is thought to be regulated by a BLUF protein, BlsA. To understand the molecular mechanism of light sensing, we have used steady-state and ultrafast vibrational spectroscopy to compare the photoactivation mechanism of BlsA to the BLUF photosensor AppA from Rhodobacter sphaeroides. Although similar photocycles are observed, vibrational data together with homology modeling identify significant differences in the β5 strand in BlsA caused by photoactivation, which are proposed to be directly linked to downstream signaling.

AB - Acinetobacter baumannii is an important human pathogen that can form biofilms and persist under harsh environmental conditions. Biofilm formation and virulence are modulated by blue light, which is thought to be regulated by a BLUF protein, BlsA. To understand the molecular mechanism of light sensing, we have used steady-state and ultrafast vibrational spectroscopy to compare the photoactivation mechanism of BlsA to the BLUF photosensor AppA from Rhodobacter sphaeroides. Although similar photocycles are observed, vibrational data together with homology modeling identify significant differences in the β5 strand in BlsA caused by photoactivation, which are proposed to be directly linked to downstream signaling.

KW - blue light using FAD

KW - BLUF domain

KW - BlsA

KW - photosensor

KW - Acinetobacter baumannii

KW - ultrafast time-resolved infrared

KW - AppA

U2 - 10.1021/jz4023738

DO - 10.1021/jz4023738

M3 - Article

SN - 1948-7185

VL - 5

SP - 220

EP - 224

JO - The Journal of Physical Chemistry Letters

JF - The Journal of Physical Chemistry Letters

IS - 1

ER -

Ultrafast structural dynamics of BlsA, a photoreceptor from the pathogenic bacterium Acinetobacter baumannii

Abstract

Keywords

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Projects

International Collaboration in Chemistry: BLUF Domain blue light photosensors a paradigm for optogenetics

Cite this