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Evolution and Multiplicity of Arginine Decarboxylases in Polyamine Biosynthesis and Essential Role in Bacillus subtilis Biofilm Formation

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Evolution and Multiplicity of Arginine Decarboxylases in Polyamine Biosynthesis and Essential Role in Bacillus subtilis Biofilm Formation. / Burrell, Matthew; Hanfrey, Colin C.; Murray, Ewan J.; Stanley-Wall, Nicola R.; Michael, Anthony J.

In: Journal of Biological Chemistry, Vol. 285, No. 50, 12.2010, p. 39224-39238.

Research output: Contribution to journalArticle

Harvard

Burrell, M, Hanfrey, CC, Murray, EJ, Stanley-Wall, NR & Michael, AJ 2010, 'Evolution and Multiplicity of Arginine Decarboxylases in Polyamine Biosynthesis and Essential Role in Bacillus subtilis Biofilm Formation' Journal of Biological Chemistry, vol 285, no. 50, pp. 39224-39238.

APA

Burrell, M., Hanfrey, C. C., Murray, E. J., Stanley-Wall, N. R., & Michael, A. J. (2010). Evolution and Multiplicity of Arginine Decarboxylases in Polyamine Biosynthesis and Essential Role in Bacillus subtilis Biofilm Formation. Journal of Biological Chemistry, 285(50), 39224-39238doi: 10.1074/jbc.M110.163154

Vancouver

Burrell M, Hanfrey CC, Murray EJ, Stanley-Wall NR, Michael AJ. Evolution and Multiplicity of Arginine Decarboxylases in Polyamine Biosynthesis and Essential Role in Bacillus subtilis Biofilm Formation. Journal of Biological Chemistry. 2010 Dec;285(50):39224-39238.

Author

Burrell, Matthew; Hanfrey, Colin C.; Murray, Ewan J.; Stanley-Wall, Nicola R.; Michael, Anthony J. / Evolution and Multiplicity of Arginine Decarboxylases in Polyamine Biosynthesis and Essential Role in Bacillus subtilis Biofilm Formation.

In: Journal of Biological Chemistry, Vol. 285, No. 50, 12.2010, p. 39224-39238.

Research output: Contribution to journalArticle

Bibtex - Download

@article{5e893504b0094c91933bc81acea77834,
title = "Evolution and Multiplicity of Arginine Decarboxylases in Polyamine Biosynthesis and Essential Role in <em>Bacillus subtilis</em> Biofilm Formation",
author = "Matthew Burrell and Hanfrey, {Colin C.} and Murray, {Ewan J.} and Stanley-Wall, {Nicola R.} and Michael, {Anthony J.}",
year = "2010",
volume = "285",
number = "50",
pages = "39224--39238",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Evolution and Multiplicity of Arginine Decarboxylases in Polyamine Biosynthesis and Essential Role in <em>Bacillus subtilis</em> Biofilm Formation

A1 - Burrell,Matthew

A1 - Hanfrey,Colin C.

A1 - Murray,Ewan J.

A1 - Stanley-Wall,Nicola R.

A1 - Michael,Anthony J.

AU - Burrell,Matthew

AU - Hanfrey,Colin C.

AU - Murray,Ewan J.

AU - Stanley-Wall,Nicola R.

AU - Michael,Anthony J.

PY - 2010/12

Y1 - 2010/12

N2 - <p>Arginine decarboxylases (ADCs; EC 4.1.1.19) from four different protein fold families are important for polyamine biosynthesis in bacteria, archaea, and plants. Biosynthetic alanine racemase fold (AR-fold) ADC is widespread in bacteria and plants. We report the discovery and characterization of an ancestral form of the AR-fold ADC in the bacterial Chloroflexi and Bacteroidetes phyla. The ancestral AR-fold ADC lacks a large insertion found in Escherichia coli and plant AR-fold ADC and is more similar to the lysine biosynthetic enzyme meso-diaminopimelate decarboxylase, from which it has evolved. An E. coli acid-inducible ADC belonging to the aspartate aminotransferase fold (AAT-fold) is involved in acid resistance but not polyamine biosynthesis. We report here that the acid-inducible AAT-fold ADC has evolved from a shorter, ancestral biosynthetic AAT-fold ADC by fusion of a response regulator receiver domain protein to the N terminus. Ancestral biosynthetic AAT-fold ADC appears to be limited to firmicute bacteria. The phylogenetic distribution of different forms of ADC distinguishes bacteria from archaea, euryarchaeota from crenarchaeota, double-membraned from single-membraned bacteria, and firmicutes from actinobacteria. Our findings extend to eight the different enzyme forms carrying out the activity described by EC 4.1.1.19. ADC gene clustering reveals that polyamine biosynthesis employs diverse and exchangeable synthetic modules. We show that in Bacillus subtilis, ADC and polyamines are essential for biofilm formation, and this appears to be an ancient, evolutionarily conserved function of polyamines in bacteria. Also of relevance to human health, we found that arginine decarboxylation is the dominant pathway for polyamine biosynthesis in human gut microbiota.</p>

AB - <p>Arginine decarboxylases (ADCs; EC 4.1.1.19) from four different protein fold families are important for polyamine biosynthesis in bacteria, archaea, and plants. Biosynthetic alanine racemase fold (AR-fold) ADC is widespread in bacteria and plants. We report the discovery and characterization of an ancestral form of the AR-fold ADC in the bacterial Chloroflexi and Bacteroidetes phyla. The ancestral AR-fold ADC lacks a large insertion found in Escherichia coli and plant AR-fold ADC and is more similar to the lysine biosynthetic enzyme meso-diaminopimelate decarboxylase, from which it has evolved. An E. coli acid-inducible ADC belonging to the aspartate aminotransferase fold (AAT-fold) is involved in acid resistance but not polyamine biosynthesis. We report here that the acid-inducible AAT-fold ADC has evolved from a shorter, ancestral biosynthetic AAT-fold ADC by fusion of a response regulator receiver domain protein to the N terminus. Ancestral biosynthetic AAT-fold ADC appears to be limited to firmicute bacteria. The phylogenetic distribution of different forms of ADC distinguishes bacteria from archaea, euryarchaeota from crenarchaeota, double-membraned from single-membraned bacteria, and firmicutes from actinobacteria. Our findings extend to eight the different enzyme forms carrying out the activity described by EC 4.1.1.19. ADC gene clustering reveals that polyamine biosynthesis employs diverse and exchangeable synthetic modules. We show that in Bacillus subtilis, ADC and polyamines are essential for biofilm formation, and this appears to be an ancient, evolutionarily conserved function of polyamines in bacteria. Also of relevance to human health, we found that arginine decarboxylation is the dominant pathway for polyamine biosynthesis in human gut microbiota.</p>

KW - S-ADENOSYLMETHIONINE DECARBOXYLASE

KW - AMINO-ACID DECARBOXYLASES

KW - X-RAY-STRUCTURE

KW - ORNITHINE-DECARBOXYLASE

KW - CRYSTAL-STRUCTURE

KW - ESCHERICHIA-COLI

KW - DIAMINOPIMELATE DECARBOXYLASE

KW - SACCHAROMYCES-CEREVISIAE

KW - SUBSTRATE-SPECIFICITY

KW - CHLAMYDOPHILA-PNEUMONIAE

U2 - 10.1074/jbc.M110.163154

DO - 10.1074/jbc.M110.163154

M1 - Article

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 50

VL - 285

SP - 39224

EP - 39238

ER -

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