Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain.

By Ralf Paul, Stefan Weiser, N. Amiot, Carmen Chan, Tilman Schirmer, Bernd Giese, U. Jenal. Genes & Development, 2004

621 citations recorded by the source corpus.

Pole development is coordinated with the Caulobacter crescentus cell cycle by two-component signaling proteins. We show that an unusual response regulator, PleD, is required for polar differentiation and is sequestered to the cell pole only when it is activated by phosphorylation. Dynamic localization of PleD to the cell pole provides a mechanism to temporally and spatially control the signaling output of PleD during development. Targeting of PleD to the cell pole is coupled to the activation of a C-terminal guanylate cyclase domain, which catalyzes the synthesis of cyclic di-guanosine monophosphate. We propose that the local action of this novel-type guanylate cyclase might constitute a general regulatory principle in bacterial growth and development.

Subfields: Endocrinology, Genetics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/d176157e42181e13f6a22c9956b5bcfa009eafe0

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Citations in the corpus

Biofilms: the matrix revisited. (2005, background): “It should be noted, however, that GGDEF and EAL proteins can be involved in cell processes other than biofilm formation [ 23 ].”
Should we stay or should we go: mechanisms and ecological consequences for biofilm dispersal (2011, background): “Furthermore, several studies suggest that, in some instances, c-di-GMP functions within local complexes formed between the DGC or PDE and a cognate adaptor that can bind c-di-GMP and direct a specific response before the signalling molecule can diffuse throughout the cel”
PilZ domain is part of the bacterial c-di-GMP binding protein (2006, neutral): “Contact: galperin@ncbi.nlm.nih.gov Supplementary information: http://www.ncbi.nlm.nih.gov/ Complete_Genomes/SigCensus/PilZ.html”
C‐di‐GMP: the dawning of a novel bacterial signalling system (2005, background): “Such inhibition by c-di-GMP has been observed for PleD (Paul et al., 2004), in which an allosteric binding site for c-di-GMP is formed jointly by the signalling and GGDEF domain (Chan et al.”
CONSEJO SUPERIOR DE INVESTIGACIONES CIENTÍFICAS (2009, background): “crescentus, la fosforilación de PleD no sólo origina una conformación activa de la proteína, como hemos comentado anteriormente, sino que también posibilita su relocalización en posiciones polares de la célula, cerca de la base del flagelo (Paul et al., 2004).”
GGDEF and EAL domains inversely regulate cyclic di‐GMP levels and transition from sessility to motility (2004, background): “As far as we can extrapolate from our data and recent findings by others (Paul et al., 2004), all those proteins might be involved in c-diGMP turnover.”