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

Stony Brook University
University of Florida
Wistar Institute
University of East Anglia
University of Pecs
Rutherford Appleton Laboratory
University of Hamburg

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

29 Scopus citations

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	Journal of Physical Chemistry Letters
Volume	5
Issue number	1
DOIs	https://doi.org/10.1021/jz4023738
State	Published - Jan 2 2014

Keywords

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

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10.1021/jz4023738

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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. Journal of Physical Chemistry Letters, 5(1), 220-224. https://doi.org/10.1021/jz4023738

@article{156e9ee21b6b4a489d5f10b691c504f1,

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

author = "Richard Brust and Allison Haigney and Andras Lukacs and Agnieszka Gil and Shahrier Hossain and Kiri Addison and Lai, \{Cheng Tsung\} and Michael Towrie and Greetham, \{Gregory M.\} and Clark, \{Ian P.\} and Boris Illarionov and Adelbert Bacher and Kim, \{Ryu Ryun\} 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",

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journal = "Journal of Physical Chemistry Letters",

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Brust, R, Haigney, A, Lukacs, A, Gil, A, Hossain, S, Addison, K, Lai, CT, Towrie, M, Greetham, GM, Clark, IP, Illarionov, B, Bacher, A, Kim, RR, Fischer, M, Simmerling, C, Meech, SR & Tonge, PJ 2014, 'Ultrafast structural dynamics of BlsA, a photoreceptor from the pathogenic bacterium Acinetobacter baumannii', 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 - AppA

KW - BlsA

KW - blue light using FAD

KW - BLUF domain

KW - photosensor Acinetobacter baumannii

KW - ultrafast time-resolved infrared

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DO - 10.1021/jz4023738

M3 - Article

AN - SCOPUS:84891793732

SN - 1948-7185

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SP - 220

EP - 224

JO - Journal of Physical Chemistry Letters

JF - Journal of Physical Chemistry Letters

IS - 1

ER -

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

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