scholarly journals GUN1 Controls Accumulation of the Plastid Ribosomal Protein S1 at the Protein Level and Interacts with Proteins Involved in Plastid Protein Homeostasis

2016 ◽  
Vol 170 (3) ◽  
pp. 1817-1830 ◽  
Author(s):  
Luca Tadini ◽  
Paolo Pesaresi ◽  
Tatjana Kleine ◽  
Fabio Rossi ◽  
Arthur Guljamow ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Protein Level ◽  
Protein Homeostasis ◽  
Ribosomal Protein S1 ◽  
Plastid Protein ◽  
Plastid Ribosomal Protein

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.

Cooperative interactions in the system ribosomes-ribosomal protein S1-polynucleotide triplets

Biochemistry ◽  
1984 ◽  
Vol 23 (26) ◽  
pp. 6522-6529 ◽  
Author(s):  
Dixie J. Goss ◽  
Lawrence J. Parkhurst ◽  
Arkesh M. Mehta ◽  
Albert J. Wahba
Keyword(s):  
Ribosomal Protein ◽  
Cooperative Interactions ◽  
Ribosomal Protein S1
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