Difference between revisions of "Main Page"

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<big>'''Paper of the month: January 2015'''</big>  
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<big>'''Paper of the month: February 2015'''</big>  
* Proteases are crucial for the maintenance of protein integrity, but also for controlling the cellular levels of specific proteins. For the [[LonA]] protease, it has so far been unknown how the protease can specifically target a selected protein as degradation target. Now, [http://www.ncbi.nlm.nih.gov/pubmed/25538299 Mukherjee et al.] form the lab of [[Daniel Kearns]] have studied the degradation of [[SwrA]], a master regulator of flagellar biosynthesis by [[LonA]]. They found that the adaptor protein [[SmiA]] is required for the productive degradation of [[SwrA]] by [[LonA]]. This regulatory mechanism is important to prevent hyperflagellation in liquid media.
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* To proliferate efficiently, cells must co-ordinate [[cell division]] with [[DNA condensation/ segregation|chromosome segregation]]. In ''B. subtilis'', the nucleoid occlusion protein [[Noc]] binds to specific DNA sequences scattered around the chromosome and helps to protect genomic integrity by coupling the initiation of division to the progression of chromosome replication and segregation. However, how it inhibits division has remained unclear. Now, [http://www.ncbi.nlm.nih.gov/pubmed/25568309 Adams et al.] from the lab of [[Jeff Errington]] demonstrate that [[Noc]] associates with the cell membrane via an N-terminal amphipathic helix. Importantly, the membrane-binding affinity of this helix is weak and requires the assembly of nucleoprotein complexes, thus establishing a mechanism for DNA-dependent activation of [[Noc]]. Furthermore, division inhibition by [[Noc]] requires recruitment of [[Noc]] binding site DNA to the cell membrane and is dependent on its ability to bind DNA and membrane simultaneously. The results suggest a simple model in which the formation of large membrane-associated nucleoprotein complexes physically occludes assembly of the [[divisome|division machinery]].
* '''Relevant ''Subti''Wiki pages:''' [[LonA]], [[SwrA]], [[SmiA]], [[proteolysis]], [[Daniel Kearns]]
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* '''Relevant ''Subti''Wiki pages:''' [[Noc]], [[Jeff Errington]], [[cell division]], [[DNA condensation/ segregation|chromosome segregation]]
<pubmed> 25538299 </pubmed>
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<pubmed>25568309</pubmed>
 
* [[Previous papers of the month]]
 
* [[Previous papers of the month]]
  

Revision as of 17:36, 4 February 2015

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Paper of the month: February 2015

  • To proliferate efficiently, cells must co-ordinate cell division with chromosome segregation. In B. subtilis, the nucleoid occlusion protein Noc binds to specific DNA sequences scattered around the chromosome and helps to protect genomic integrity by coupling the initiation of division to the progression of chromosome replication and segregation. However, how it inhibits division has remained unclear. Now, Adams et al. from the lab of Jeff Errington demonstrate that Noc associates with the cell membrane via an N-terminal amphipathic helix. Importantly, the membrane-binding affinity of this helix is weak and requires the assembly of nucleoprotein complexes, thus establishing a mechanism for DNA-dependent activation of Noc. Furthermore, division inhibition by Noc requires recruitment of Noc binding site DNA to the cell membrane and is dependent on its ability to bind DNA and membrane simultaneously. The results suggest a simple model in which the formation of large membrane-associated nucleoprotein complexes physically occludes assembly of the division machinery.
  • Relevant SubtiWiki pages: Noc, Jeff Errington, cell division, chromosome segregation

David William Adams, Ling Juan Wu, Jeff Errington
Nucleoid occlusion protein Noc recruits DNA to the bacterial cell membrane.
EMBO J: 2015, 34(4);491-501
[PubMed:25568309] [WorldCat.org] [DOI] (I p)


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