S-glutathionylation uncouples eNOS and regulates its cellular and  vascular function pp1115 - 1118
The enzyme eNOS is crucial for regulating vascular function as it can  produce both the vasodilator nitric oxide and the vasoconstrictor  superoxide. Here it is shown that a modification associated with  oxidant stress, S-glutathionylation, switches the enzyme from forming  nitric oxide to forming superoxide. In hypertensive vessels, S- glutathionylation of eNOS is increased and this is associated with  impaired endothelium-dependent vasodilation.
Chun-An Chen et al.
doi:10.1038/nature09599
Abstract: http://www.nature.com/nature/journal/v468/n7327/abs/nature09599.html
Article: http://www.nature.com/nature/journal/v468/n7327/full/nature09599.html

Suppression of inflammation by a synthetic histone mimic pp1119 - 1123
Post-translationally modified histones are recognized by effector  proteins which contain specific binding modules; for example, the  bromodomain-containing BET proteins bind acetylated lysine residues  during gene activation. Here a synthetic small molecule is described  that interferes with the binding of certain BET family members to  acetylated histones. The compound inhibits activation of pro- inflammatory genes in macrophages and has activity in a mouse model of  inflammatory disease.
Edwige Nicodeme et al.
doi:10.1038/nature09589
Abstract: http://www.nature.com/nature/journal/v468/n7327/abs/nature09589.html
Article: http://www.nature.com/nature/journal/v468/n7327/full/nature09589.html

Transcriptional activation of polycomb-repressed genes by ZRF1 pp1124  - 1128
Ubiquitination of histone H2A has been implicated in polycomb-mediated  transcriptional silencing, but its precise functions are unclear.  Here, ZRF1 is shown to be recruited to ubiquitinated H2A and to  function in displacing polycomb-repressive complex 1 (PRC1) from  chromatin to facilitate transcriptional activation.
Holger Richly et al.
doi:10.1038/nature09574
Abstract: http://www.nature.com/nature/journal/v468/n7327/abs/nature09574.html
Article: http://www.nature.com/nature/journal/v468/n7327/full/nature09574.html

Neurotransmitter/sodium symporter orthologue LeuT has a single high- affinity substrate site pp1129 - 1132
The initial crystal structure of LeuT, together with subsequent  functional and structural studies, provided direct evidence for a  single, high-affinity substrate-binding site. Recent binding, flux and  molecular simulation studies, however, have been interpreted in terms  of a model where there are two high-affinity binding sites: the second  (S2) site is believed to be located within the extracellular  vestibule. Here, direct measurement is performed of substrate binding  to wild-type LeuT and to S2 site mutants using isothermal titration  calorimetry, equilibrium dialysis and scintillation proximity assays.  The conclusion is made that LeuT harbours a single, centrally located,  high-affinity substrate-binding site.
Chayne L. Piscitelli, Harini Krishnamurthy and Eric Gouaux
doi:10.1038/nature09581
Abstract: http://www.nature.com/nature/journal/v468/n7327/abs/nature09581.html
Article: http://www.nature.com/nature/journal/v468/n7327/full/nature09581.html
 

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