2 Matching Annotations
  1. Jul 2018
    1. On 2015 Dec 15, Martine Crasnier-Mednansky commented:

      This article is remarkable for demonstrating an interaction between unphosphorylated Enzyme IIA<sup>Glc</sup> and the EAL domain of CsrD. Such interaction is physiologically connected to the role of cAMP in E. coli because there is an established correlation between the phosphorylation state of Enzyme IIA<sup>Glc</sup> and the level of cAMP, phosphorylation of Enzyme IIA<sup>Glc</sup> typically causing an increase in the cAMP level (and concomitantly eliminating the effect of Enzyme IIA<sup>Glc</sup> on CsrD).

      The authors discussed the present regulatory interaction with no mention to the role of cAMP. However, considering (1) the inhibitory function of (CsrD-controlled) CsrA on glycogen biosynthesis, (2) the ability of stationary-phase E. coli to accumulate glycogen as a carbon reserve, and (3) the increase in cAMP occurring upon entry into the stationary phase (because of Enzyme IIA<sup>Glc</sup> phosphorylation) (MAKMAN RS, 1965), it seems CsrD and CRP-cAMP both work 'in concert' for the timeliness of physiological processes during entry into stationary phase, particularly when cells are growing on glucose.


      This comment, imported by Hypothesis from PubMed Commons, is licensed under CC BY.

  2. Feb 2018
    1. On 2015 Dec 15, Martine Crasnier-Mednansky commented:

      This article is remarkable for demonstrating an interaction between unphosphorylated Enzyme IIA<sup>Glc</sup> and the EAL domain of CsrD. Such interaction is physiologically connected to the role of cAMP in E. coli because there is an established correlation between the phosphorylation state of Enzyme IIA<sup>Glc</sup> and the level of cAMP, phosphorylation of Enzyme IIA<sup>Glc</sup> typically causing an increase in the cAMP level (and concomitantly eliminating the effect of Enzyme IIA<sup>Glc</sup> on CsrD).

      The authors discussed the present regulatory interaction with no mention to the role of cAMP. However, considering (1) the inhibitory function of (CsrD-controlled) CsrA on glycogen biosynthesis, (2) the ability of stationary-phase E. coli to accumulate glycogen as a carbon reserve, and (3) the increase in cAMP occurring upon entry into the stationary phase (because of Enzyme IIA<sup>Glc</sup> phosphorylation) (MAKMAN RS, 1965), it seems CsrD and CRP-cAMP both work 'in concert' for the timeliness of physiological processes during entry into stationary phase, particularly when cells are growing on glucose.


      This comment, imported by Hypothesis from PubMed Commons, is licensed under CC BY.