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DEAD-Box RNA Helicases in Bacillus subtilis Have Multiple Functions and Act Independently from Each Other
Author(s) -
Martin LehnikHabrink,
Leonie Rempeters,
Ákos T. Kovács,
Christoph Wrede,
Claudia Baierlein,
Heike Krebber,
Oscar P. Kuipers,
Jörg Stülke
Publication year - 2012
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.01475-12
Subject(s) - biology , rna , ribosome biogenesis , helicase , bacillus subtilis , eif4a , rna helicase a , degradosome , ribosome , non coding rna , biogenesis , microbiology and biotechnology , exosome complex , genetics , rna binding protein , gene , bacteria
DEAD-box RNA helicases play important roles in remodeling RNA molecules and in facilitating a variety of RNA-protein interactions that are key to many essential cellular processes. In spite of the importance of RNA, our knowledge about RNA helicases is limited. In this study, we investigated the role of the four DEAD-box RNA helicases in the Gram-positive model organism Bacillus subtilis. A strain deleted of all RNA helicases is able to grow at 37°C but not at lower temperatures. The deletion of cshA, cshB, or yfmL in particular leads to cold-sensitive phenotypes. Moreover, these mutant strains exhibit unique defects in ribosome biogenesis, suggesting distinct functions for the individual enzymes in this process. Based on protein accumulation, severity of the cold-sensitive phenotype, and the interaction with components of the RNA degradosome, CshA is the major RNA helicase of B. subtilis. To unravel the functions of CshA in addition to ribosome biogenesis, we conducted microarray analysis and identified the ysbAB and frlBONMD mRNAs as targets that are strongly affected by the deletion of the cshA gene. Our findings suggest that the different helicases make distinct contributions to the physiology of B. subtilis. Ribosome biogenesis and RNA degradation are two of their major tasks in B. subtilis.

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