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1.
PLoS Pathog ; 17(5): e1009617, 2021 05.
Artigo em Inglês | MEDLINE | ID: mdl-34043736

RESUMO

Urinary tract infections (UTIs) are a common bacterial infectious disease in humans, and strains of uropathogenic Escherichia coli (UPEC) are the most frequent cause of UTIs. During infection, UPEC must cope with a variety of stressful conditions in the urinary tract. Here, we demonstrate that the small RNA (sRNA) RyfA of UPEC strains is required for resistance to oxidative and osmotic stresses. Transcriptomic analysis of the ryfA mutant showed changes in expression of genes associated with general stress responses, metabolism, biofilm formation and genes coding for cell surface proteins. Inactivation of ryfA in UPEC strain CFT073 decreased urinary tract colonization in mice and the ryfA mutant also had reduced production of type 1 and P fimbriae (pili), adhesins which are known to be important for UTI. Furthermore, loss of ryfA also reduced UPEC survival in human macrophages. Thus, ryfA plays a key regulatory role in UPEC adaptation to stress, which contributes to UTI and survival in macrophages.


Assuntos
Biofilmes/crescimento & desenvolvimento , Infecções por Escherichia coli/microbiologia , Pequeno RNA não Traduzido/genética , Infecções Urinárias/microbiologia , Escherichia coli Uropatogênica/genética , Adaptação Fisiológica , Adesinas Bacterianas/genética , Adesinas Bacterianas/metabolismo , Animais , Fímbrias Bacterianas/metabolismo , Perfilação da Expressão Gênica , Humanos , Macrófagos/microbiologia , Camundongos , Osmorregulação , Estresse Oxidativo , RNA Bacteriano/genética , Deleção de Sequência , Escherichia coli Uropatogênica/crescimento & desenvolvimento , Escherichia coli Uropatogênica/fisiologia , Virulência
2.
Trends Genet ; 37(1): 86-97, 2021 01.
Artigo em Inglês | MEDLINE | ID: mdl-33077249

RESUMO

RNA binding proteins (RBPs) are ubiquitously found in all kingdoms of life. They are involved in a plethora of regulatory events, ranging from direct regulation of gene expression to guiding modification of RNA molecules. As bacterial regulators, RBPs can act alone or in concert with RNA-based regulators, such as small regulatory RNAs (sRNAs), riboswitches, or clustered regularly interspaced short palindromic repeats (CRISPR) RNAs. Various functions of RBPs, whether dependent or not on an RNA regulator, have been described in the past. However, the past decade has been a fertile ground for the development of novel high-throughput methods. These methods acted as stepping-stones for the discovery of new functions of RBPs and helped in the understanding of the molecular mechanisms behind previously described regulatory events. Here, we present an overview of the recently identified roles of major bacterial RBPs from different model organisms. Moreover, the tight relationship between RBPs and RNA-based regulators will be explored.


Assuntos
Bactérias/genética , Sistemas CRISPR-Cas , Regulação Bacteriana da Expressão Gênica , RNA Bacteriano/genética , Pequeno RNA não Traduzido/genética , Proteínas de Ligação a RNA/metabolismo , Bactérias/metabolismo , Proteínas de Ligação a RNA/genética
3.
Nat Commun ; 11(1): 5609, 2020 11 05.
Artigo em Inglês | MEDLINE | ID: mdl-33154383

RESUMO

Polycomb Group (PcG) proteins organize chromatin at multiple scales to regulate gene expression. A conserved Sterile Alpha Motif (SAM) in the Polycomb Repressive Complex 1 (PRC1) subunit Polyhomeotic (Ph) has been shown to play an important role in chromatin compaction and large-scale chromatin organization. Ph SAM forms helical head to tail polymers, and SAM-SAM interactions between chromatin-bound Ph/PRC1 are believed to compact chromatin and mediate long-range interactions. To understand the underlying mechanism, here we analyze the effects of Ph SAM on chromatin in vitro. We find that incubation of chromatin or DNA with a truncated Ph protein containing the SAM results in formation of concentrated, phase-separated condensates. Ph SAM-dependent condensates can recruit PRC1 from extracts and enhance PRC1 ubiquitin ligase activity towards histone H2A. We show that overexpression of Ph with an intact SAM increases ubiquitylated H2A in cells. Thus, SAM-induced phase separation, in the context of Ph, can mediate large-scale compaction of chromatin into biochemical compartments that facilitate histone modification.


Assuntos
Proteínas de Ligação a DNA/química , Proteínas de Drosophila/química , Complexo Repressor Polycomb 1/química , Proteínas do Grupo Polycomb/metabolismo , Motivo Estéril alfa/fisiologia , Animais , Compartimento Celular , Linhagem Celular , Núcleo Celular/metabolismo , Cromatina/metabolismo , DNA/metabolismo , Proteínas de Ligação a DNA/genética , Proteínas de Ligação a DNA/metabolismo , Drosophila , Proteínas de Drosophila/genética , Proteínas de Drosophila/metabolismo , Histonas/metabolismo , Complexo Repressor Polycomb 1/genética , Complexo Repressor Polycomb 1/metabolismo , Polimerização , Motivo Estéril alfa/genética , Ubiquitinação
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