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- W2000490869 abstract "Copper resistance system in the cyanobacterium Synechocystis sp. PCC 6803 comprises two operons, copMRS and copBAC, which are expressed in response to copper in the media. copBAC codes for a heavy-metal efflux–resistance nodulation and division (HME-RND) system, while copMRS codes for a protein of unknown function, CopM, and a two-component system CopRS, which controls the expression of these two operons. Here, we report that CopM is a periplasmic protein able to bind Cu(I) with high affinity (KD ~3 × 10−16). Mutants lacking copM showed a sensitive copper phenotype similar to mutants affected in copB, but lower than mutants of the two-component system CopRS, suggesting that CopBAC and CopM constitute two independent resistance mechanisms. Moreover, constitutive expression of copM is able to partially suppress the copper sensitivity of the copR mutant strain, pointing out that CopM per se is able to confer copper resistance. Furthermore, constitutive expression of copM was able to reduce total cellular copper content of the copR mutant to the levels determined in the wild-type (WT) strain. Finally, CopM was localized not only in the periplasm but also in the extracellular space, suggesting that CopM can also prevent copper accumulation probably by direct copper binding outside the cell." @default.
- W2000490869 created "2016-06-24" @default.
- W2000490869 creator A5021700963 @default.
- W2000490869 creator A5027403999 @default.
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- W2000490869 date "2014-12-26" @default.
- W2000490869 modified "2023-10-16" @default.
- W2000490869 title "CopM is a novel copper‐binding protein involved in copper resistance in <i> <scp>S</scp> ynechocystis </i> sp. <scp>PCC</scp> 6803" @default.
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- W2000490869 doi "https://doi.org/10.1002/mbo3.231" @default.
- W2000490869 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4335983" @default.
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