Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

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Translocase malfunction causes extracellular protein translocation stress ( EPTS) in Streptomyces lividans


ABSTRACT: The genomic and proteomic analyses of Streptomyces lividans strains deficient in the major signal peptidase SipY or in the translocase complex protein SecG resulted in a set of genes being equally regulated. These genes are apparently responsible for the common deficiencies in extracellular protein production and sporulation shared by both mutant strains, constituting a cellular response to the stress caused by the potential malfunction of the translocase complex, which we have named M-bM-^@M-^\extracellular protein translocation stress (EPTS)M-bM-^@M-^]. All microarray analyses were performed with RNA samples obtained from three independent cultures grown under identical conditions. The cDNA obtained from each RNA preparation of the SipY-deficient strain or the SecG-deficient strain were hybridised with the cDNA obtained from the equivalent RNA preparation of the wild type strain (S. lividans TK21).

ORGANISM(S): Streptomyces lividans

SUBMITTER: Sonia GullM-CM-3n 

PROVIDER: E-GEOD-17012 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Publications

Translocase and major signal peptidase malfunctions affect aerial mycelium formation in Streptomyces lividans.

Gullón Sonia S   Palomino Carmen C   Navajas Rosana R   Paradela Alberto A   Mellado Rafael P RP  

Journal of biotechnology 20120413 3-4


Deficiency in the translocase complex (SecG mutant strain) or in the major type I signal peptidase (SipY mutant strain) function in Streptomyces lividans resulted, as expected, in a drastic reduction of secretory protein production and in a bald phenotype. The transcriptional profiling of both strains showed that the expression of a set of genes involved in the morphological differentiation process was down regulated in both mutant strains (bldG, bldN and bldM), whereas bldA and bldH were only d  ...[more]

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