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Contributions of protein structure and gene position to the compartmentalization of the regulatory proteins σ E and SpoIIE in sporulating Bacillus subtilis
Author(s) -
McBride Shonna M.,
Rubio Aileen,
Wang Lei,
Haldenwang William G.
Publication year - 2005
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2005.04712.x
Subject(s) - biology , sigma factor , compartment (ship) , bacillus subtilis , compartmentalization (fire protection) , microbiology and biotechnology , transcription (linguistics) , rna polymerase , gene , gene expression , rna , genetics , biochemistry , enzyme , oceanography , linguistics , philosophy , bacteria , geology
Summary At an early stage in endospore formation Bacillus subtilis partitions itself into two dissimilar compartments with unique developmental fates. Transcription appropriate to each compartment is initiated by the activation of compartment‐specific RNA polymerase sigma subunits, σ E in the mother cell and σ F in the forespore. Among the possible factors contributing to the compartment specificity of σ E and σ F is the selective accumulation of the σ E protein in the mother cell and that of SpoIIE, a regulatory phosphatase essential to the activation of σ F , in the forespore. In the current work, fluorescent microscopy is used to investigate the contributions of σ E and SpoIIE's protein structures, expression and the genetic asymmetry that develops during chromosome translocation into the forespore on their abundance in each compartment. Time of entry of the spoIIE and sigE genes into the forespore was found to have a significant effect on the enrichment of their products in one or the other compartment. In contrast, the structures of the proteins themselves do not appear to promote their transfer to a particular compartment, but nonetheless contribute to compartmentalization by facilitating degradation in the compartment where each protein's activity would be inappropriate.