scholarly journals Translation inhibition from a distance: The small RNA SgrS silences a ribosomal protein S1‐dependent enhancer

2020 ◽  
Vol 114 (3) ◽  
pp. 391-408 ◽  
Author(s):  
Muhammad S. Azam ◽  
Carin K. Vanderpool
Keyword(s):  
Ribosomal Protein ◽  
Small Rna ◽  
Translation Inhibition ◽  
Ribosomal Protein S1

scholarly journals Translation inhibition from a distance: the small RNA SgrS interferes with a ribosomal protein S1-dependent enhancer

2019 ◽  
Author(s):  
Muhammad S. Azam ◽  
Carin K. Vanderpool
Keyword(s):  
Ribosomal Protein ◽  
Translational Regulation ◽  
Ribosomal Subunit ◽  
Start Codon ◽  
Binding Interaction ◽  
Translation Inhibition ◽  
Ribosomal Protein S1 ◽  
Chaperone Protein ◽  
Ribosomal Subunit Protein ◽  
Mrna Binding

SummaryMany bacterial small RNAs (sRNAs) efficiently inhibit translation of target mRNAs by forming a duplex that sequesters the Shine-Dalgarno (SD) sequence or start codon and prevents formation of the translation initiation complex. There are a growing number of examples of sRNA-mRNA binding interactions distant from the SD region, but how these mediate translational regulation remains unclear. Our previous work in Escherichia coli and Salmonella identified a mechanism of translational repression of manY mRNA by the sRNA SgrS through a binding interaction upstream of the manY SD. Here, we report that SgrS forms a duplex with a uridine-rich translation-enhancing element in the manY 5’ untranslated region. Notably, we show that the enhancer is ribosome-dependent and that the small ribosomal subunit protein S1 interacts with the enhancer to promote translation of manY. In collaboration with the chaperone protein Hfq, SgrS interferes with the interaction between the translation enhancer and ribosomal protein S1 to repress translation of manY mRNA. Since bacterial translation is often modulated by enhancer-like elements upstream of the SD, sRNA-mediated enhancer silencing could be a common mode of gene regulation.

scholarly journals Recognition of RNA by ribosomal protein S1: Interaction of S1 with 23 S rRNA of Escherichia coli

FEBS Letters ◽  
1977 ◽  
Vol 80 (2) ◽  
pp. 255-260 ◽  
Author(s):  
Alain Krol ◽  
Christiane Branlant ◽  
Jean-Pierre Ebel ◽  
Louis Peter Visentin
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Ribosomal Protein S1

scholarly journals An A/U-Rich Enhancer Region Is Required for High-Level Protein Secretion through the HlyA Type I Secretion System

2017 ◽  
Vol 84 (1) ◽  
Author(s):  
Sakshi Khosa ◽  
Romy Scholz ◽  
Christian Schwarz ◽  
Mirko Trilling ◽  
Hartmut Hengel ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Protein Secretion ◽  
Fusion Proteins ◽  
Untranslated Region ◽  
Secretion System ◽  
Type I ◽  
Secretion Systems ◽  
Enhancer Region ◽  
Ribosomal Protein S1 ◽  
Cellular Expression

ABSTRACTEfficient protein secretion is often a valuable alternative to classic cellular expression to obtain homogenous protein samples. Early on, bacterial type I secretion systems (T1SS) were employed to allow heterologous secretion of fusion proteins. However, this approach was not fully exploited, as many proteins could not be secreted at all or only at low levels. Here, we present an engineered microbial secretion system which allows the effective production of proteins up to a molecular mass of 88 kDa. This system is based on the hemolysin A (HlyA) T1SS of the Gram-negative bacteriumEscherichia coli, which exports polypeptides when fused to a hemolysin secretion signal. We identified an A/U-rich enhancer region upstream ofhlyArequired for effective expression and secretion of selected heterologous proteins irrespective of their prokaryotic, viral, or eukaryotic origin. We further demonstrate that the ribosomal protein S1 binds to thehlyAA/U-rich enhancer region and that this region is involved in the high yields of secretion of functional proteins, like maltose-binding protein or human interferon alpha-2.IMPORTANCEA 5′ untranslated region of the mRNA of substrates of type I secretion systems (T1SS) drastically enhanced the secretion efficiency of the endogenously secreted protein. The identification of ribosomal protein S1 as the interaction partner of this 5′ untranslated region provides a rationale for the enhancement. This strategy furthermore can be transferred to fusion proteins allowing a broader, and eventually a more general, application of this system for secreting heterologous fusion proteins.

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