Affiliation:
1. Lehrstuhl für Mikrobiologie, Institut für Mikrobiologie, Biochemie und Genetik der Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany,1 and
2. Laboratory for Microbiology, E. C. Slater Institute, BioCentrum Amsterdam, 1018 WS Amsterdam, The Netherlands2
Abstract
ABSTRACT
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 ς
70
promoter, and an
estB-oxyR
containing message is also transcribed from an internal promoter.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology