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Journal of Bacteriology, May 2000, p. 2967-2969, Vol. 182, No. 10
Institut Cavanilles de Biodiversitat i
Biologia Evolutiva and Departament de Genètica, Universitat
de València, 46071 València, Spain
Received 18 November 1999/Accepted 18 February 2000
Buchnera aphidicola, the prokaryotic endosymbiont of
aphids, complements dietary deficiencies with the synthesis and
provision of several essential amino acids. We have cloned and
sequenced a region of the genome of B. aphidicola isolated
from Acyrthosiphon pisum which includes the two-domain
aroQ/pheA gene. This gene encodes the bifunctional
chorismate mutase-prephenate dehydratase protein, which plays a central
role in L-phenylalanine biosynthesis. Two changes involved
in the overproduction of this amino acid have been detected. First, the
absence of an attenuator region suggests a constitutive expression of
this gene. Second, the regulatory domain of the Buchnera
prephenate dehydratase shows changes in the ESRP sequence, which is
involved in the allosteric binding of phenylalanine and is strongly
conserved in prephenate dehydratase proteins from practically all known
organisms. These changes suggest the desensitization of the enzyme to
inhibition by phenylalanine and would permit the bacterial endosymbiont
to overproduce phenylalanine.
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Prephenate Dehydratase from the Aphid Endosymbiont
(Buchnera) Displays Changes in the Regulatory Domain That
Suggest Its Desensitization to Inhibition by Phenylalanine
*
Corresponding author. Mailing address: Institut
Cavanilles de Biodiversitat i Biologia Evolutiva, Universitat de
València, Apartat 22085, 46071 Valencia, Spain.
E-mail: francisco.silva{at}uv.es.
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