Chai Yunrong, Kolter Roberto, Losick Richard
Department of Molecular and Cellular Biology, the Biological Laboratories, Harvard University, Cambridge, MA 02138, USA.
J Bacteriol. 2009 Apr;191(8):2423-30. doi: 10.1128/JB.01464-08. Epub 2009 Feb 6.
We report that catabolism of l-lactate in Bacillus subtilis depends on the previously uncharacterized yvfV-yvfW-yvbY (herein renamed lutABC) operon, which is inferred to encode three iron-sulfur-containing proteins. The operon is under the dual control of a GntR-type repressor (LutR, formerly YvfI) and the master regulator for biofilm formation SinR and is induced during growth in response to l-lactate. Operons with high similarity to lutABC are present in the genomes of a variety of gram-positive and gram-negative bacteria, raising the possibility that LutABC is a widely conserved and previously unrecognized pathway for the utilization of l-lactate or related metabolites.
我们报告称,枯草芽孢杆菌中L-乳酸的分解代谢依赖于先前未被鉴定的yvfV-yvfW-yvbY(在此重新命名为lutABC)操纵子,据推测该操纵子编码三种含硫铁蛋白。该操纵子受GntR型阻遏物(LutR,原YvfI)和生物膜形成的主要调节因子SinR的双重控制,并在L-乳酸存在的生长过程中被诱导。与lutABC高度相似的操纵子存在于多种革兰氏阳性和革兰氏阴性细菌的基因组中,这增加了LutABC是一种广泛保守且先前未被认识的L-乳酸或相关代谢物利用途径的可能性。