Susan J. Dorrian
Commonwealth Scientific and Industrial Research Organisation
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Featured researches published by Susan J. Dorrian.
Applied and Environmental Microbiology | 2010
Gunjan Pandey; Susan J. Dorrian; Robyn J. Russell; Clint Brearley; Steven Kotsonis; John G. Oakeshott
ABSTRACT A highly efficient carbendazim (methyl-1H-benzimidazol-2-ylcarbamate, or MBC)-mineralizing bacterium was isolated from enrichment cultures originating from MBC-contaminated soil samples. This bacterium, Nocardioides sp. strain SG-4G, hydrolyzed MBC to 2-aminobenzimidazole, which in turn was converted to the previously unknown metabolite 2-hydroxybenzimidazole. The initial steps of this novel metabolic pathway were confirmed by growth and enzyme assays and liquid chromatography-mass spectrometry (LC-MS) studies. The enzyme responsible for carrying out the first step was purified and subjected to N-terminal and internal peptide sequencing. The cognate gene, named mheI (for MBC-hydrolyzing enzyme), was cloned using a reverse genetics approach. The MheI enzyme was found to be a serine hydrolase of 242 amino acid residues. Its nearest known relative is an uncharacterized hypothetical protein with only 40% amino acid identity to it. Codon optimized mheI was heterologously expressed in Escherichia coli, and the His-tagged enzyme was purified and biochemically characterized. The enzyme has a Km and kcat of 6.1 μM and 170 min−1, respectively, for MBC. Radiation-killed, freeze-dried SG-4G cells showed strong and stable MBC detoxification activity suitable for use in enzymatic bioremediation applications.
Microbial Biotechnology | 2015
Matthew Wilding; Ellen F. A. Walsh; Susan J. Dorrian; Colin Scott
A Pseudomonas species [Pseudomonas sp. strain amino alkanoate catabolism (AAC)] was identified that has the capacity to use 12‐aminododecanoic acid, the constituent building block of homo‐nylon‐12, as a sole nitrogen source. Growth of Pseudomonas sp. strain AAC could also be supported using a range of additional ω‐amino alkanoates. This metabolic function was shown to be most probably dependent upon one or more transaminases (TAs). Fourteen genes encoding putative TAs were identified from the genome of Pseudomonas sp. AAC. Each of the 14 genes was cloned, 11 of which were successfully expressed in Escherichia coli and tested for activity against 12‐aminododecanoic acid. In addition, physiological functions were proposed for 9 of the 14 TAs. Of the 14 proteins, activity was demonstrated in 9, and of note, 3 TAs were shown to be able to catalyse the transfer of the ω‐amine from 12‐aminododecanoic acid to pyruvate. Based on this study, three enzymes have been identified that are promising biocatalysts for the production of nylon and related polymers.
Journal of Bacteriology | 2011
Stephen L. Pearce; Rinku Pandey; Susan J. Dorrian; Robyn J. Russell; John G. Oakeshott; Gunjan Pandey
Strain SG-6C (DSM 23264, CCM 7827) is a chemolithoautotrophic bacterium of the family Bradyrhizobiaceae. It can also grow heterotrophically under appropriate environmental conditions. Here we report the annotated genome sequence of this strain in a single 4.3-Mb circular scaffold.
PLOS ONE | 2012
Madhura Shettigar; Stephen L. Pearce; Rinku Pandey; Fazlurrahman Khan; Susan J. Dorrian; Sahil Balotra; Robyn J. Russell; John G. Oakeshott; Gunjan Pandey
A 6-chloronicotinic acid mineralizing bacterium was isolated from enrichment cultures originating from imidacloprid-contaminated soil samples. This Bradyrhizobiaceae, designated strain SG-6C, hydrolytically dechlorinated 6-chloronicotinic acid to 6-hydroxynicotinic acid, which was then further metabolised via the nicotinic acid pathway. This metabolic pathway was confirmed by growth and resting cell assays using HPLC and LC-MS studies. A candidate for the gene encoding the initial dechlorination step, named cch2 (for 6-chloronicotinic acid chlorohydrolase), was identified using genome sequencing and its function was confirmed using resting cell assays on E. coli heterologously expressing this gene. The 464 amino acid enzyme was found to be a member of the metal dependent hydrolase superfamily with similarities to the TRZ/ATZ family of chlorohydrolases. We also provide evidence that cch2 was mobilized into this bacterium by an Integrative and Conjugative Element (ICE) that feeds 6-hydroxynicotinic acid into the existing nicotinic acid mineralization pathway.
Biochemical and Biophysical Research Communications | 2009
Gunjan Pandey; Susan J. Dorrian; Robyn J. Russell; John G. Oakeshott
Insect Biochemistry and Molecular Biology | 2005
Rama Heidari; A.L. Devonshire; B.E. Campbell; Susan J. Dorrian; John G. Oakeshott; Robyn J. Russell
Insect Biochemistry and Molecular Biology | 2004
R. Heidari; A.L. Devonshire; B.E. Campbell; K.L. Bell; Susan J. Dorrian; John G. Oakeshott; Dr.R.J. Russell
Journal of General Virology | 1995
Terry N. Hanzlik; Susan J. Dorrian; Karyn N. Johnson; Elizabeth M. Brooks; Karl H.J. Gordon
Journal of General Virology | 1993
Terry N. Hanzlik; Susan J. Dorrian; Karl H.J. Gordon; Peter D. Christian
Journal of Invertebrate Pathology | 2002
Elizabeth M. Brooks; Karl H.J. Gordon; Susan J. Dorrian; Eric R. Hines; Terry N. Hanzlik
Collaboration
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Commonwealth Scientific and Industrial Research Organisation
View shared research outputsCommonwealth Scientific and Industrial Research Organisation
View shared research outputsCommonwealth Scientific and Industrial Research Organisation
View shared research outputsCommonwealth Scientific and Industrial Research Organisation
View shared research outputsCommonwealth Scientific and Industrial Research Organisation
View shared research outputsCommonwealth Scientific and Industrial Research Organisation
View shared research outputsCommonwealth Scientific and Industrial Research Organisation
View shared research outputsCommonwealth Scientific and Industrial Research Organisation
View shared research outputsCommonwealth Scientific and Industrial Research Organisation
View shared research outputsCommonwealth Scientific and Industrial Research Organisation
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