scholarly journals Bacillus thuringiensispeptidoglycan hydrolase SleB171 involved in daughter cell separation during cell division

2016 ◽  
Vol 48 (4) ◽  
pp. 354-362 ◽  
Author(s):  
Hua Li ◽  
Penggao Hu ◽  
Xiuyun Zhao ◽  
Ziniu Yu ◽  
Lin Li
mBio ◽  
2016 ◽  
Vol 7 (4) ◽  
Author(s):  
Xiaoxue Zhou ◽  
David K. Halladin ◽  
Julie A. Theriot

ABSTRACT Dividing cells of the coccoid Gram-positive bacterium Staphylococcus aureus undergo extremely rapid (millisecond) daughter cell separation (DCS) driven by mechanical crack propagation, a strategy that is very distinct from the gradual, enzymatically driven cell wall remodeling process that has been well described in several rod-shaped model bacteria. To determine if other bacteria, especially those in the same phylum ( Firmicutes ) or with similar coccoid shapes as S. aureus , might use a similar mechanically driven strategy for DCS, we used high-resolution video microscopy to examine cytokinesis in a phylogenetically wide range of species with various cell shapes and sizes. We found that fast mechanically driven DCS is rather rare in the Firmicutes (low G+C Gram positives), observed only in Staphylococcus and its closest coccoid relatives in the Macrococcus genus, and we did not observe this division strategy among the Gram-negative Proteobacteria . In contrast, several members of the high-G+C Gram-positive phylum Actinobacteria ( Micrococcus luteus , Brachybacterium faecium , Corynebacterium glutamicum , and Mycobacterium smegmatis ) with diverse shapes ranging from coccoid to rod all undergo fast mechanical DCS during cell division. Most intriguingly, similar fast mechanical DCS was also observed during the sporulation of the actinobacterium Streptomyces venezuelae . IMPORTANCE Much of our knowledge on bacterial cytokinesis comes from studying rod-shaped model organisms such as Escherichia coli and Bacillus subtilis . Less is known about variations in this process among different bacterial species. While cell division in many bacteria has been characterized to some extent genetically or biochemically, few species have been examined using video microscopy to uncover the kinetics of cytokinesis and daughter cell separation (DCS). In this work, we found that fast (millisecond) DCS is exhibited by species in two independent clades of Gram-positive bacteria and is particularly prevalent among the Actinobacteria , a diverse group that includes significant pathogens as well as bacteria that generate medically important antibiotics.


Structure ◽  
2010 ◽  
Vol 18 (9) ◽  
pp. 1184-1190 ◽  
Author(s):  
Alessia Ruggiero ◽  
Daniela Marasco ◽  
Flavia Squeglia ◽  
Silvia Soldini ◽  
Emilia Pedone ◽  
...  

Science ◽  
2015 ◽  
Vol 348 (6234) ◽  
pp. 574-578 ◽  
Author(s):  
X. Zhou ◽  
D. K. Halladin ◽  
E. R. Rojas ◽  
E. F. Koslover ◽  
T. K. Lee ◽  
...  

2017 ◽  
Vol 199 (14) ◽  
Author(s):  
Atsushi Yahashiri ◽  
Matthew A. Jorgenson ◽  
David S. Weiss

ABSTRACT Sporulation-related repeat (SPOR) domains are small peptidoglycan (PG) binding domains found in thousands of bacterial proteins. The name “SPOR domain” stems from the fact that several early examples came from proteins involved in sporulation, but SPOR domain proteins are quite diverse and contribute to a variety of processes that involve remodeling of the PG sacculus, especially with respect to cell division. SPOR domains target proteins to the division site by binding to regions of PG devoid of stem peptides (“denuded” glycans), which in turn are enriched in septal PG by the intense, localized activity of cell wall amidases involved in daughter cell separation. This targeting mechanism sets SPOR domain proteins apart from most other septal ring proteins, which localize via protein-protein interactions. In addition to SPOR domains, bacteria contain several other PG-binding domains that can exploit features of the cell wall to target proteins to specific subcellular sites.


2016 ◽  
Vol 22 (6) ◽  
pp. 477-486 ◽  
Author(s):  
Catherine Chaput ◽  
Chantal Ecobichon ◽  
Nadine Pouradier ◽  
Jean-Claude Rousselle ◽  
Abdelkader Namane ◽  
...  

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