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and genetic characterization of dca genes required for beta-oxidation of straight-chain dicarboxylic acids in Acinetobacter sp. strain ADP1. Appl Environ Microbiol 2001, 67:4817–4827.PubMedCrossRef Competing interests The authors declare that they have no competing interests. Authors’ contributions Conceived and designed the experiments: PPDN, FR, MG, MT, and RZ. Performed the experiments and analyzed the data: FR, PPDN, and MG. Wrote the paper: PPDN and RZ. All authors read and approved the final manuscript.”
“Background The species Streptococcus thermophilus is a Lactic Acid Bacterium (LAB) used as a starter of fermentation in yogurt and cheese production. In nature
and during Adenylyl cyclase dairy fermentation processes, S. thermophilus is subjected to sudden changes in its environment and its industrial performance is conditioned by its ability to successfully adapt to harsh conditions. To survive, like many other bacteria, this species must develop appropriate physiological responses by modifying gene expression appropriately. One of the stresses, that S. thermophilus AG-881 cost commonly encounters, is the modification of the temperature. For instance, during the production of dairy products, temperature shifts are applied to regulate the bacterial growth and, thus, control the lactic acid production [1]. S. thermophilus survival against thermal stress is conditioned by its ability to sense and quickly adapt its physiology mainly by the synthesis of adequate proteins at the right moment. For example, adaptation of S. thermophilus to a lowering of temperature required the synthesis of a set of chaperones called cold shock proteins (Csp) that is strongly induced in response to a rapid decrease in growth temperature [2, 3]. As in other Gram positive bacteria, S. thermophilus also responds to thermal stress by synthesizing a conserved set of heat-shock proteins (Hsp), including both chaperones and proteases [4]. Their role during heat stress is to rescue, or to scavenge, heat-denatured proteins.