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Journal of Bacteriology, July 1999, p. 4292-4298, Vol. 181, No. 14
Lehrstuhl für Mikrobiologie, Institut
für Mikrobiologie, Biochemie und Genetik der
Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany,1 and Laboratory for
Microbiology, E. C. Slater Institute, BioCentrum Amsterdam,
1018 WS Amsterdam, The Netherlands2
Received 12 February 1999/Accepted 5 May 1999
Alkanes are oxidized in Acinetobacter sp. strain ADP1
by a three-component alkane monooxygenase, composed of alkane
hydroxylase, rubredoxin, and rubredoxin reductase. rubA and
rubB encode rubredoxin and a NAD(P)H-dependent rubredoxin
reductase. We demonstrate here that single base pair substitutions in
rubA or rubB lead to defects in alkane
degradation, showing that both genes are essential for alkane
utilization. Differences in the degradation capacity for hexadecane and
dodecane in these mutants are discussed. Two genes, estB
and oxyR, are located downstream of rubB, but
are not necessary for alkane degradation. estB encodes a
functional esterase. oxyR encodes a LysR-type
transcriptional regulator, conferring resistance to hydrogen peroxide.
rubA, rubB, estB, and
oxyR constitute an operon, which is constitutively
transcribed from a
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
The Genes rubA and rubB for
Alkane Degradation in Acinetobacter sp. Strain ADP1 Are in
an Operon with estB, Encoding an Esterase, and
oxyR
70 promoter, and an
estB-oxyR containing message is also transcribed from an
internal promoter.
*
Corresponding author. Mailing address: Lehrstuhl
für Mikrobiologie, Institut für Mikrobiologie, Biochemie
und Genetik der Friedrich-Alexander-Universität
Erlangen-Nürnberg, Staudtstrasse 5, 91058 Erlangen, Germany.
Phone: 49 (9131) 8528081. Fax: 49 (9131) 8528082. E-mail:
whillen{at}biologie.uni-erlangen.de.
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