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Journal of Bacteriology, September 1999, p. 5766-5770, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Acylhomoserine Lactone Synthase Activity of the
Vibrio fischeri AinS Protein
Brian L.
Hanzelka,1
Matthew R.
Parsek,1
Dale L.
Val,2
Paul V.
Dunlap,3
John E.
Cronan Jr.,2,4 and
E. P.
Greenberg1,*
Department of Microbiology, University of
Iowa, Iowa City, Iowa 522421; Department
of Microbiology2 and Department of
Biochemistry,4 University of Illinois, Urbana,
Illinois 61801; and Center of Marine Biotechnology,
University of Maryland Biotechnology Institute, Baltimore, Maryland
212023
Received 26 April 1999/Accepted 8 July 1999
Acylhomoserine lactones, which serve as quorum-sensing signals in
gram-negative bacteria, are produced by members of the LuxI family of
synthases. LuxI is a Vibrio fischeri enzyme that catalyzes the synthesis of N-(3-oxohexanoyl)-L-homoserine
lactone from an acyl-acyl carrier protein and
S-adenosylmethionine. Another V. fischeri gene,
ainS, directs the synthesis of
N-octanoylhomoserine lactone. The AinS protein shows no
significant sequence similarity with LuxI family members, but it does
show sequence similarity with the Vibrio harveyi LuxM
protein. The luxM gene is required for the synthesis of
N-(3-hydroxybutyryl)-L-homoserine lactone. To
gain insights about whether AinS and LuxM represent a second family of
acylhomoserine lactone synthases, we have purified AinS as a
maltose-binding protein (MBP) fusion protein. The purified MBP-AinS
fusion protein catalyzed the synthesis of
N-octanoylhomoserine lactone from
S-adenosylmethionine and either octanoyl-acyl carrier protein or, to a lesser extent, octanoyl coenzyme A. With the exception
that octanoyl coenzyme A served as an acyl substrate for the MBP-AinS
fusion protein, the substrates for and reaction kinetics of the
MBP-AinS fusion protein were similar to those of the several LuxI
family members previously studied. We conclude that AinS is an
acylhomoserine lactone synthase and that it represents a second family
of such enzymes.
*
Corresponding author. Mailing address: Department of
Microbiology, University of Iowa, Iowa City, IA 52242. Phone: (319)
335-7775. Fax: (319) 335-7949. E-mail:
epgreen{at}blue.weeg.uiowa.edu.
Journal of Bacteriology, September 1999, p. 5766-5770, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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