Biosynthesis of storage compounds by Rhodococcus jostii RHA1 and global identification of genes involved in their metabolism.
BACKGROUND
Members of the genus Rhodococcus are frequently found in soil and other natural environments and are highly resistant to stresses common in those environments. The accumulation of storage compounds permits cells to survive and metabolically adapt during fluctuating environmental conditions. The purpose of this study was to perform a genome-wide bioinformatic analysis of key genes encoding metabolism of diverse storage compounds by Rhodococcus jostii RHA1 and to examine its ability to synthesize and accumulate triacylglycerols (TAG), wax esters, polyhydroxyalkanoates (PHA), glycogen and polyphosphate (PolyP).


RESULTS
We identified in the RHA1 genome: 14 genes encoding putative wax ester synthase/acyl-CoA:diacylglycerol acyltransferase enzymes (WS/DGATs) likely involved in TAG and wax esters biosynthesis; a total of 54 genes coding for putative lipase/esterase enzymes possibly involved in TAG and wax ester degradation; 3 sets of genes encoding PHA synthases and PHA depolymerases; 6 genes encoding key enzymes for glycogen metabolism, one gene coding for a putative polyphosphate kinase and 3 putative exopolyphosphatase genes. Where possible, key amino acid residues in the above proteins (generally in active sites, effectors binding sites or substrate binding sites) were identified in order to support gene identification. RHA1 cells grown under N-limiting conditions, accumulated TAG as the main storage compounds plus wax esters, PHA (with 3-hydroxybutyrate and 3-hydroxyvalerate monomers), glycogen and PolyP. Rhodococcus members were previously known to accumulate TAG, wax esters, PHAs and polyP, but this is the first report of glycogen accumulation in this genus.


CONCLUSIONS
RHA1 possess key genes to accumulate diverse storage compounds. Under nitrogen-limiting conditions lipids are the principal storage compounds. An extensive capacity to synthesize and metabolize storage compounds appears to contribute versatility to RHA1 in its responses to environmental stresses.
Hernández
Martín A
MA
Centro Regional de Investigación y Desarrollo Científico Tecnológico, Facultad de Ciencias Naturales, Universidad Nacional de Patagonia San Juan Bosco, Km 4-Ciudad Universitaria, 9000 Comodoro Rivadavia, Chubut, Argentina. mahernandez@unpata.edu.ar
Mohn
William W
WW
Martínez
Eliana
E
Rost
Enrique
E
Alvarez
Adrián F
AF
Alvarez
Héctor M
HM
D000217:Acyltransferases / Q000235:genetics; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics; D051048:Diacylglycerol O-Acyltransferase / Q000235:genetics; D004950:Esterases / Q000235:genetics; D005798:Genes, Bacterial; D006003:Glycogen / Q000096:biosynthesis; D008049:Lipase / Q000235:genetics; D008055:Lipids / Q000096:biosynthesis; D008969:Molecular Sequence Data; D054813:Polyhydroxyalkanoates / Q000096:biosynthesis; D011122:Polyphosphates / Q000378:metabolism; D012240:Rhodococcus / Q000235:genetics* / Q000378:metabolism*; D016415:Sequence Alignment; D014280:Triglycerides / Q000096:biosynthesis; D014885:Waxes / Q000378:metabolism
D001426:Bacterial Proteins; D008055:Lipids; D054813:Polyhydroxyalkanoates; D011122:Polyphosphates; D014280:Triglycerides; D014885:Waxes; D006003:Glycogen; D000217:Acyltransferases; D051048:Diacylglycerol O-Acyltransferase; C079165:long-chain-alcohol O-fatty-acyltransferase; D004950:Esterases; D008049:Lipase