Abstract:
:ecs is a three-cistron operon of Bacillus subtilis, encoding proteins with similarity to the ATPase (EcsA) and hydrophobic components (EcsB) of ABC transporters. The ecsA26 point mutation was shown to cause a strong processing defect of a secreted alpha-amylase precursor (preAmyQ) and of three other exoproteins. Northern analysis of the level of amyQ mRNA showed that ecsA26 also decreases amyQ transcription. This effect too was pleiotropic, as judged by a drastic decrease in the expression from an exoprotease promoter of a reporter protein. A knockout mutation of the ecsB cistron caused a processing defect similar to ecsA26 but, unlike ecsA26, did not affect amyQ transcription. These was also no defect in transcription in the ecsA ecsB double mutant. Thus, an intact ecsB product was required for the downregulation of amyQ by the mutant ecsA. These results suggest a dual regulatory function for Ecs, in which Ecs, possibly as part of a signal transduction mechanism, regulates some component(s) of the protein secretion apparatus as well as secretory protein transcription in a co-ordinated fashion.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Leskelä S,Wahlström E,Hyyryläinen HL,Jacobs M,Palva A,Sarvas M,Kontinen VPdoi
10.1046/j.1365-2958.1999.01194.xsubject
Has Abstractpub_date
1999-01-01 00:00:00pages
533-43issue
2eissn
0950-382Xissn
1365-2958journal_volume
31pub_type
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