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Local adaptation is ubiquitous, but the molecular mechanisms giving rise to this ecological phenomenon remain largely unknown. A year-long reciprocal transplant of mustard hill coral (Porites astreoides) between a highly environmentally variable inshore habitat and more stable offshore habitat demonstrated that both inshore and offshore populations exhibit elevated growth, protein and lipid content in their home reef environment, indicative of local adaptation. Here, we characterized the genomic basis of this adaptation in both coral hosts and their intracellular algal symbionts (Symbiodinium sp.) using genome-wide gene expression profiling and gene coexpression network analysis. Inshore and offshore coral populations differ primarily in their capacity for gene expression plasticity: upon transplantation to a novel environment inshore corals were able to match expression profiles of the local population significantly better than offshore corals. Furthermore, elevated plasticity in expression of environmental stress response (ESR) genes was adaptive in the inshore environment: it correlated with the least susceptibility to a natural summer bleaching event, whereas higher constitutive ESR gene expression (\"frontloading\" sensu Barshis et al. 2013) did not. Our results reveal a novel genomic mechanism of resilience to a variable environment, demonstrating that corals are capable of a more diverse molecular response to environmental stress than previously thought.

Abstract The structural gene of the carboxypeptidase T (cpt) was successfully expressed in cell wall-less L-form cells of Proteus mirabilis. The DNA sequence encoding the PhoA leader peptide was fused with a truncated cpt gene encoding the mature enzyme. The modified gene in a pUC-based kanamycin resistance vector under the control of the lac promoter was transformed into L-form cells of P. mirabilis. They were able to produce the recombinant CpT both as a secretory and as a cell-bound insoluble form. The co-secretory processing of the PhoA leader peptide was quite efficient. The yield of the secreted CpT was not less than 20 mg l−1 and should be improvable.

The structural gene of the carboxypeptidase T ( cpt) was successfully expressed in cell wall-less L-form cells of Proteus mirabilis. The DNA sequence encoding the PhoA leader peptide was fused with a truncated cpt gene encoding the mature enzyme. The modified gene in a pUC-based kanamycin resistance vector under the control of the lac promoter was transformed into L-form cells of P. mirabilis. They were able to produce the recombinant CpT both as a secretory and as a cell-bound insoluble form. The co-secretory processing of the PhoA leader peptide was quite efficient. The yield of the secreted CpT was not less than 20 mg l −1 and should be improvable.