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A superfamily of proteins that contain the cold-shock domain.
Members of a family of cold-shock proteins (CSPs) are found throughout the eubacterial domain and appear to function as RNA-chaperones. They have been implicated in various cellular processes,Expand
Cold shock stress-induced proteins in Bacillus subtilis.
Bacteria respond to a decrease in temperature with the induction of proteins that are classified as cold-induced proteins (CIPs). Using two-dimensional gel electrophoresis, we analyzed the cold shockExpand
Cell cycle‐dependent localization of two novel prokaryotic chromosome segregation and condensation proteins in Bacillus subtilis that interact with SMC protein
Disruption of ypuG and ypuH open reading frames in Bacillus subtilis leads to temperature‐sensitive slow growth, a defect in chromosome structure and formation of anucleate cells. The genes, whichExpand
A family of cold shock proteins in Bacillus subtilis is essential for cellular growth and for efficient protein synthesis at optimal and low temperatures
Like other bacteria, Bacillus subtilis possesses a family of homologous small acidic proteins (CspB, CspC and CspD, identity > 70%) that are strongly induced in response to cold shock. We show thatExpand
Intracellular Protein and DNA Dynamics in Competent Bacillus subtilis Cells
We have found that two DNA repair/recombination proteins localize differentially to the cell poles in competent Bacillus subtilis cells. RecA protein colocalized with competence protein ComGA, andExpand
Dynamic movement of actin‐like proteins within bacterial cells
Actin proteins are present in pro‐ and eukaryotes, and have been shown to perform motor‐like functions in eukaryotic cells in a variety of processes. Bacterial actin homologues are essential for cellExpand
Bacterial translation elongation factor EF-Tu interacts and colocalizes with actin-like MreB protein
We show that translation initiation factor EF-Tu plays a second important role in cell shape maintenance in the bacterium Bacillus subtilis. EF-Tu localizes in a helical pattern underneath the cellExpand
Cold-induced putative DEAD box RNA helicases CshA and CshB are essential for cold adaptation and interact with cold shock protein B in Bacillus subtilis.
The nucleic acid binding cold shock proteins (CSPs) and the cold-induced DEAD box RNA helicases have been proposed separately to act as RNA chaperones, but no experimental evidence has been reportedExpand
Use of time‐lapse microscopy to visualize rapid movement of the replication origin region of the chromosome during the cell cycle in Bacillus subtilis
We describe the use of time‐lapse fluorescence microscopy to visualize the movement of the DNA replication origin and terminus regions on the Bacillus subtilis chromosome during the course of theExpand
Actin-like Proteins MreB and Mbl from Bacillus subtilis Are Required for Bipolar Positioning of Replication Origins
Actin-like proteins MreB and Mbl are required for proper cell shape and for viability in B. subtilis and form dynamic helical filaments underneath the cell membrane. We have found that depletion ofExpand