The regulon of the RNA chaperone CspA and its auto-regulation in Staphylococcus aureus
Fecha
2018Autor
Versión
Acceso abierto / Sarbide irekia
Tipo
Artículo / Artikulua
Versión
Versión publicada / Argitaratu den bertsioa
Identificador del proyecto
Impacto
|
10.1093/nar/gkx1284
Resumen
RNA-binding proteins (RBPs) are essential to finetune
gene expression. RBPs containing the coldshock
domain are RNA chaperones that have been
extensively studied. However, the RNA targets and
specific functions for many of them remain elusive.
Here, combining comparative proteomics and RBPimmunoprecipitation-
microarray profiling, we have
determined the regulon of the RNA chaperone CspA
o ...
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RNA-binding proteins (RBPs) are essential to finetune
gene expression. RBPs containing the coldshock
domain are RNA chaperones that have been
extensively studied. However, the RNA targets and
specific functions for many of them remain elusive.
Here, combining comparative proteomics and RBPimmunoprecipitation-
microarray profiling, we have
determined the regulon of the RNA chaperone CspA
of Staphylococcus aureus. Functional analysis revealed
that proteins involved in carbohydrate and ribonucleotide
metabolism, stress response and virulence
gene expression were affected by cspA
deletion. Stress-associated phenotypes such as increased
bacterial aggregation and diminished resistance
to oxidative-stress stood out. Integration of
the proteome and targetome showed that CspA posttranscriptionally
modulates both positively and negatively
the expression of its targets, denoting additional
functions to the previously proposed translation
enhancement. One of these repressed targets
was its own mRNA, indicating the presence of a
negative post-transcriptional feedback loop. CspA
bound the 5 UTR of its own mRNA disrupting a hairpin,
which was previously described as an RNase III
target. Thus, deletion of the cspA 5 UTR abrogated
mRNA processing and auto-regulation. We propose
that CspA interacts through a U-rich motif, which
is located at the RNase III cleavage site, portraying
CspA as a putative RNase III-antagonist. [--]
Materias
RNA chaperone CspA,
Staphylococcus aureus
Editor
Oxford University Press
Publicado en
Nucleic Acids Research, 2018, Vol. 46, No. 3 1345–1361
Departamento
Universidad Pública de Navarra/Nafarroako Unibertsitate Publikoa. IdAB. Instituto de Agrobiotecnología / Agrobioteknologiako Institutua
Versión del editor
Entidades Financiadoras
European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation programme [646869]; Spanish Ministry of Economy and Competitiveness [BFU2011-23222, BIO2014-53530-R, BFU2014-56698-P]; Spanish National Research Council [CSIC-PII-201540I013]; C.J.C. was supported by predoctoral contract from the Public University of Navarre (UPNA), Spain. Funding for open access charge: European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation programme [646869].
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