Difference between revisions of "Papers of the month"

From SubtiWiki
Jump to: navigation, search
(2013)
Line 8: Line 8:
  
 
* '''August 2013'''
 
* '''August 2013'''
** In cells, the concentration of ribonucleotides by far exceeds that of deoxyribonucleotides. This poses problems since the DNA polymerase incorporates one rNTP every 2.3 kb during [[DNA replication|chromosome replication]]. Now, [http://www.ncbi.nlm.nih.gov/pubmed/23882084 Yao et al.] investigated how these misincorporations  are repaired. The demonstrate that this repair is initiated by [[rnhB|RNase HII]] that nicks DNA at single rNMP residues to initiate replacement with dNMP.
+
** In cells, the concentration of ribonucleotides by far exceeds that of deoxyribonucleotides. This poses problems since the DNA polymerase incorporates one rNTP every 2.3 kb during [[DNA replication|chromosome replication]]. Now, [http://www.ncbi.nlm.nih.gov/pubmed/23882084 Yao et al.] investigated how these misincorporations  are repaired. They demonstrate that this repair is initiated by [[rnhB|RNase HII]] that nicks DNA at single rNMP residues to initiate replacement with dNMPs.
 
** '''Relevant ''Subti''Wiki pages:'''  [[DNA replication]], [[DNA repair/ recombination|DNA repair]], ''[[rnhB]]'', ''[[rnhC]]'', ''[[mutS]]'', ''[[mutL]]''
 
** '''Relevant ''Subti''Wiki pages:'''  [[DNA replication]], [[DNA repair/ recombination|DNA repair]], ''[[rnhB]]'', ''[[rnhC]]'', ''[[mutS]]'', ''[[mutL]]''
 
<pubmed> 23882084 </pubmed>
 
<pubmed> 23882084 </pubmed>
  
 
* '''July 2013'''
 
* '''July 2013'''
** Ca(2+) efflux by Ca(2+) cation antiporter (CaCA) proteins is important for maintenance of Ca(2+) homeostasis across the cell membrane. Now, [http://www.ncbi.nlm.nih.gov/pubmed/23798403 Wu et al.] determined the structure of the B. subtilis Ca(2+)/H(+) antiporter protein [[ChaA]]. By structural and mutational analyses, they establish structural bases for mechanisms of Ca(2+)/H(+) exchange and its pH regulation. Moreover, this work also sheds light on the evolutionary adaptation to different energy modes in the CaCA protein family.
+
** Ca<sup>2+</sup> efflux by Ca<sup>2+</sup> cation antiporter (CaCA) proteins is important for maintenance of Ca<sup>2+</sup> homeostasis across the cell membrane. Now, [http://www.ncbi.nlm.nih.gov/pubmed/23798403 Wu et al.] determined the structure of the ''B. subtilis'' Ca<sup>2+</sup>/H<sup>+</sup> antiporter protein [[ChaA]]. By structural and mutational analyses, they establish structural bases for mechanisms of Ca<sup>2+</sup>/H<sup>+</sup> exchange and its pH regulation. Moreover, this work also sheds light on the evolutionary adaptation to different energy modes in the CaCA protein family.
 
** '''Relevant ''Subti''Wiki pages:'''  [[ChaA]], [[membrane proteins]], [[metal ion homeostasis (K, Na, Ca, Mg)]]
 
** '''Relevant ''Subti''Wiki pages:'''  [[ChaA]], [[membrane proteins]], [[metal ion homeostasis (K, Na, Ca, Mg)]]
 
<pubmed> 23798403 </pubmed>
 
<pubmed> 23798403 </pubmed>
  
 
* '''June 2013'''
 
* '''June 2013'''
** DNA transfer across membranes is important in many fundamental processes. However, the molecular mechanisms behind this transport are only poorly understood. Now, [http://www.ncbi.nlm.nih.gov/pubmed/23667326 Fiche et al.] analysed the assembly and molecular architecture of the [[SpoIIIE]] DNA translocation complex. This study reveals that in contrast to previous model, DNA transfer occurs through an aqueous DNA-conducting pore that could be structurally maintained by the divisional machinery, with [[SpoIIIE]] acting as a checkpoint preventing membrane fusion until completion of chromosome segregation.  
+
** DNA transfer across membranes is important in many fundamental processes. However, the molecular mechanisms behind this transport are only poorly understood. Now, [http://www.ncbi.nlm.nih.gov/pubmed/23667326 Fiche et al.] analysed the assembly and molecular architecture of the [[SpoIIIE]] DNA translocation complex. This study reveals that in contrast to a previous model, DNA transfer occurs through an aqueous DNA-conducting pore that could be structurally maintained by the divisional machinery, with [[SpoIIIE]] acting as a checkpoint preventing membrane fusion until completion of chromosome segregation.  
 
** '''Relevant ''Subti''Wiki pages:'''  [[sporulation]], [[SpoIIIE]], [[DNA condensation/ segregation]]
 
** '''Relevant ''Subti''Wiki pages:'''  [[sporulation]], [[SpoIIIE]], [[DNA condensation/ segregation]]
 
<pubmed> 23667326 </pubmed>
 
<pubmed> 23667326 </pubmed>
Line 28: Line 28:
  
 
* '''April 2013'''
 
* '''April 2013'''
** Usually, [[cell wall synthesis]] is regarded as being essential for ''B. subtilis''. Now, [http://www.ncbi.nlm.nih.gov/pubmed/23452849 Mercier et al.] from the lab of [[Jeff Errington]] show that excess biosynthesis of membranes is sufficient to drive the formation of cell wall-less L-forms in B. subtilis. Interestingly, this cell form is even independent of the essential [[cell division]] protein [[FtsZ]].
+
** Usually, [[cell wall synthesis]] is regarded as being essential for ''B. subtilis''. Now, [http://www.ncbi.nlm.nih.gov/pubmed/23452849 Mercier et al.] from the lab of [[Jeff Errington]] show that excess biosynthesis of membranes is sufficient to drive the formation of cell wall-less L-forms in ''B. subtilis''. Interestingly, this cell form is even independent of the essential [[cell division]] protein [[FtsZ]].
 
** '''Relevant ''Subti''Wiki pages:'''  [[Jeff Errington]], [[biosynthesis of lipids]], [[cell wall synthesis]], [[cell division]], [[FtsZ]]
 
** '''Relevant ''Subti''Wiki pages:'''  [[Jeff Errington]], [[biosynthesis of lipids]], [[cell wall synthesis]], [[cell division]], [[FtsZ]]
 
<pubmed> 23452849 </pubmed>
 
<pubmed> 23452849 </pubmed>
Line 40: Line 40:
  
 
* '''February 2013'''
 
* '''February 2013'''
** For many [[essential genes]] of ''B. subtilis'', it is not clear why they are essential in ''B. subtilis'' but not in closely related species. Strikingly, this is the case for [[RNases]] such as RNases [[rnc|III]] and [[rny|Y]]. Now, [http://www.ncbi.nlm.nih.gov/pubmed/23300471 Durand et al.] from the lab of [[Ciaran Condon]] have identified the reason for the essentiality of [[rnc|RNase III]]: This enzyme is required to degrade phage encoded toxin mRNA molecules thus protecting the cell from lysis caused by the encoded toxins. Indeed, [[rnc|RNase III]] is dispensable in a strain lacking the [[Skin element]] and the [[SPß prophage]] that harbor the corresponding toxin genes.
+
** For many [[essential genes]] of ''B. subtilis'', it is not clear why they are essential in ''B. subtilis'' but not in closely related species. Strikingly, this is the case for [[RNases]] such as [[RNases]] [[rnc|III]] and [[rny|Y]]. Now, [http://www.ncbi.nlm.nih.gov/pubmed/23300471 Durand et al.] from the lab of [[Ciaran Condon]] have identified the reason for the essentiality of [[rnc|RNase III]]: This enzyme is required to degrade phage encoded toxin mRNA molecules thus protecting the cell from lysis caused by the encoded toxins. Indeed, [[rnc|RNase III]] is dispensable in a strain lacking the [[Skin element]] and the [[SPß prophage]] that harbor the corresponding toxin genes.
 
** '''Relevant ''Subti''Wiki pages:'''  [[Ciaran Condon]], [[rnc|RNase III]], [[essential genes]], ''[[yonT]]'', ''[[txpA]]'', [[toxins, antitoxins and immunity against toxins]]
 
** '''Relevant ''Subti''Wiki pages:'''  [[Ciaran Condon]], [[rnc|RNase III]], [[essential genes]], ''[[yonT]]'', ''[[txpA]]'', [[toxins, antitoxins and immunity against toxins]]
 
<pubmed> 23300471 </pubmed>
 
<pubmed> 23300471 </pubmed>
Line 49: Line 49:
  
 
* '''January 2013'''
 
* '''January 2013'''
** [http://www.ncbi.nlm.nih.gov/pubmed/23267091 Castaing et al..] from the lab of [[Kumaran Ramamurthi]] show how ATP hydrolysis drives the self-association of [[SpoIVA]] into nucleotide-free filaments which then serve as a platform for the assembly of the spore coat starting with [[SpoVM]]. Together with the [http://www.ncbi.nlm.nih.gov/pubmed/23167435 december's paper of the month] these works demonstrate how ATP hydrolysis may contribute to different process wihtin a potein such as global conformational changes and self-assembly.
+
** [http://www.ncbi.nlm.nih.gov/pubmed/23267091 Castaing et al.] from the lab of [[Kumaran Ramamurthi]] show how ATP hydrolysis drives the self-association of [[SpoIVA]] into nucleotide-free filaments which then serve as a platform for the assembly of the spore coat starting with [[SpoVM]]. Together with the [http://www.ncbi.nlm.nih.gov/pubmed/23167435 december's paper of the month] these works demonstrate how ATP hydrolysis may contribute to different processes within a protein such as global conformational changes and self-assembly.
 
** '''Relevant ''Subti''Wiki pages:'''  [[Kumaran Ramamurthi]], [[SpoIVA]], [[sporulation]]
 
** '''Relevant ''Subti''Wiki pages:'''  [[Kumaran Ramamurthi]], [[SpoIVA]], [[sporulation]]
 
<pubmed> 23267091 </pubmed>
 
<pubmed> 23267091 </pubmed>
Line 55: Line 55:
 
=2012=
 
=2012=
 
* '''December 2012'''
 
* '''December 2012'''
** [http://www.ncbi.nlm.nih.gov/pubmed/23167435 Kim et al..] show how the ATP hydrolysis controls the global conformation of the [[SecA]] translocase and drives [[protein secretion]]. The intricate network of structural interactions, which couple local electrostatic changes during ATP hydrolysis to global conformational and dynamic changes in [[SecA]], form the foundation of the allosteric mechanochemistry that efficiently harnesses the chemical energy stored in ATP to drive complex mechanical processes.
+
** [http://www.ncbi.nlm.nih.gov/pubmed/23167435 Kim et al.] show how the ATP hydrolysis controls the global conformation of the [[SecA]] translocase and drives [[protein secretion]]. The intricate network of structural interactions, which couple local electrostatic changes during ATP hydrolysis to global conformational and dynamic changes in [[SecA]], form the foundation of the allosteric mechanochemistry that efficiently harnesses the chemical energy stored in ATP to drive complex mechanical processes.
 
** '''Relevant ''Subti''Wiki pages:'''  [[SecA]], [[protein secretion]]
 
** '''Relevant ''Subti''Wiki pages:'''  [[SecA]], [[protein secretion]]
 
<pubmed> 23167435 </pubmed>
 
<pubmed> 23167435 </pubmed>

Revision as of 19:57, 28 August 2013

2013

  • September 2013
    • Biofilms of B. subtilis consist of cells in a matrix made up of extracellular polysaccharides, the amyloid-like TasA protein, and the hydrophobic protein BslA. Now, Hobley et al. from the lab of Nicola Stanley-Wall determined the structure of BslA and found that the protein has an extremely hydrophobic cap domain that acts like a raincoat for the biofilm. The authors suggest that BslA is a bacterial hydrophobin.
    • Relevant SubtiWiki pages: Nicola Stanley-Wall, biofilm formation, BslA

  • A comment on this paper:


  • August 2013
    • In cells, the concentration of ribonucleotides by far exceeds that of deoxyribonucleotides. This poses problems since the DNA polymerase incorporates one rNTP every 2.3 kb during chromosome replication. Now, Yao et al. investigated how these misincorporations are repaired. They demonstrate that this repair is initiated by RNase HII that nicks DNA at single rNMP residues to initiate replacement with dNMPs.
    • Relevant SubtiWiki pages: DNA replication, DNA repair, rnhB, rnhC, mutS, mutL


  • July 2013
    • Ca2+ efflux by Ca2+ cation antiporter (CaCA) proteins is important for maintenance of Ca2+ homeostasis across the cell membrane. Now, Wu et al. determined the structure of the B. subtilis Ca2+/H+ antiporter protein ChaA. By structural and mutational analyses, they establish structural bases for mechanisms of Ca2+/H+ exchange and its pH regulation. Moreover, this work also sheds light on the evolutionary adaptation to different energy modes in the CaCA protein family.
    • Relevant SubtiWiki pages: ChaA, membrane proteins, metal ion homeostasis (K, Na, Ca, Mg)


  • June 2013
    • DNA transfer across membranes is important in many fundamental processes. However, the molecular mechanisms behind this transport are only poorly understood. Now, Fiche et al. analysed the assembly and molecular architecture of the SpoIIIE DNA translocation complex. This study reveals that in contrast to a previous model, DNA transfer occurs through an aqueous DNA-conducting pore that could be structurally maintained by the divisional machinery, with SpoIIIE acting as a checkpoint preventing membrane fusion until completion of chromosome segregation.
    • Relevant SubtiWiki pages: sporulation, SpoIIIE, DNA condensation/ segregation


  • May 2013
    • Paul et al. demonstrate that the orientation of the genes on the chromosome has a significant impact on their evolution: Gene encoded on the lagging strand evolve faster than those on the leading strand. This faster evolution is caused by collisions between the DNA replication and transcription machineries that result in DNA damage and subsequent fixation of errors as mutations. Importantly, essential genes are strongly underrepresented on the lagging strand thus providing a "built-in" protection of the encoded important proteins against possible deleterious mutations.
    • Relevant SubtiWiki pages: transcription, DNA replication, essential genes



  • March 2013
    • The mechanism of membrane fission in bacteria has been a long-standing enigma. Now, Doan et al. from the lab of David Rudner demonstrate how the FisB protein (previously YunB) mediates membrane fission during sporulation This activity of FisB is based on its ability to bind to lipids, specifically to cardiolipin.
    • Relevant SubtiWiki pages: David Rudner, FisB, sporulation

  • See also:


  • A comment on this paper:

  • See also:



2012

  • December 2012
    • Kim et al. show how the ATP hydrolysis controls the global conformation of the SecA translocase and drives protein secretion. The intricate network of structural interactions, which couple local electrostatic changes during ATP hydrolysis to global conformational and dynamic changes in SecA, form the foundation of the allosteric mechanochemistry that efficiently harnesses the chemical energy stored in ATP to drive complex mechanical processes.
    • Relevant SubtiWiki pages: SecA, protein secretion










  • A comment on these papers:


  • A comment on this paper:



2011






  • A comment on these papers:



  • May 2011
    • Miles et al. identified the enzyme for the key final step in the biosynthesis of queuosine, a hypermodified base found in the wobble positions of tRNA Asp, Asn, His, and Tyr from bacteria to man
    • Relevant SubtiWiki pages: QueG, translation