the ruegeria pomeroyi acui gene has a role in dmsp catabolism and resembles yhdh of e. coli and other bacteria in conferring resistance to acrylate的ruegeria pomeroyi acui基因dmsp分解代谢作用,类似于yhdh大肠杆菌和其它细菌的丙烯酸酯产生抗性.pdfVIP
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the ruegeria pomeroyi acui gene has a role in dmsp catabolism and resembles yhdh of e. coli and other bacteria in conferring resistance to acrylate的ruegeria pomeroyi acui基因dmsp分解代谢作用,类似于yhdh大肠杆菌和其它细菌的丙烯酸酯产生抗性
The Ruegeria pomeroyi acuI Gene Has a Role in DMSP
Catabolism and Resembles yhdH of E. coli and Other
Bacteria in Conferring Resistance to Acrylate
Jonathan D. Todd, Andrew R. J. Curson, Matthew J. Sullivan, Mark Kirkwood, Andrew W. B. Johnston*
School of Biological Sciences, University of East Anglia, Norwich, United Kingdom
Abstract
The Escherichia coli YhdH polypeptide is in the MDR012 sub-group of medium chain reductase/dehydrogenases, but its
biological function was unknown and no phenotypes of YhdH2 mutants had been described. We found that an E. coli strain
with an insertional mutation in yhdH was hyper-sensitive to inhibitory effects of acrylate, and, to a lesser extent, to those of
3-hydroxypropionate. Close homologues of YhdH occur in many Bacterial taxa and at least two animals. The acrylate
sensitivity of YhdH2 mutants was corrected by the corresponding, cloned homologues from several bacteria. One such
homologue is acuI, which has a role in acrylate degradation in marine bacteria that catabolise dimethylsulfoniopropionate
(DMSP) an abundant anti-stress compound made by marine phytoplankton. The acuI genes of such bacteria are often linked
to ddd genes that encode enzymes that cleave DMSP into acrylate plus dimethyl sulfide (DMS), even though these are in
different polypeptide families, in unrelated bacteria. Furthermore, most strains of Roseobacters, a clade of abundant marine
bacteria, cleave DMSP into acrylate plus DMS, and can also demethylate it, using DMSP demethylase. In most Roseobacters,
the corresponding gene, dmdA, lies immediately upstream of acuI and in the model Roseobacter strain Ruegeria pomeroyi
DSS-3, dmdA-acuI were co-regulated in response to the co-inducer, acrylate. These observations, together with findings by
others that AcuI has acryloyl-CoA reductase activity, lead us to suggest that Yd
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