scholarly journals Identification of Protein Synthesis Elongation Factor G as a 4.5 S RNA-binding Protein inEscherichia coli

1996 ◽  
Vol 271 (22) ◽  
pp. 13162-13168 ◽  
Author(s):  
Toshinori Shibata ◽  
Yasuyuki Fujii ◽  
Yoshio Nakamura ◽  
Kouji Nakamura ◽  
Kunio Yamane
Keyword(s):  
Protein Synthesis ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Elongation Factor ◽  
Inescherichia Coli ◽  
Elongation Factor G ◽  
Factor G

2′,3′-Cyclic nucleotide 3′-phosphodiesterase: A novel RNA-binding protein that inhibits protein synthesis

2009 ◽  
Vol 87 (5) ◽  
pp. 1069-1079 ◽  
Author(s):  
Michel Gravel ◽  
Francis Robert ◽  
Vicky Kottis ◽  
Imed-Eddine Gallouzi ◽  
Jerry Pelletier ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Cyclic Nucleotide ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein

scholarly journals Translational Repression by RNA-Binding Protein TIAR

2006 ◽  
Vol 26 (7) ◽  
pp. 2716-2727 ◽  
Author(s):  
Krystyna Mazan-Mamczarz ◽  
Ashish Lal ◽  
Jennifer L. Martindale ◽  
Tomoko Kawai ◽  
Myriam Gorospe
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Protein Biosynthesis ◽  
Rna Binding Protein ◽  
Elongation Factor ◽  
Initiation Factor ◽  
Translation Elongation ◽  
Initiation Factors ◽  
Translation Initiation Factors ◽  
Cellular Translation

ABSTRACT The RNA-binding protein TIAR has been proposed to inhibit protein synthesis transiently by promoting the formation of translationally silent stress granules. Here, we report the selective binding of TIAR to several mRNAs encoding translation factors such as eukaryotic initiation factor 4A (eIF4A) and eIF4E (translation initiation factors), eEF1B (a translation elongation factor), and c-Myc (which transcriptionally controls the expression of numerous translation regulatory proteins). TIAR bound the 3′-untranslated regions of these mRNAs and potently suppressed their translation, particularly in response to low levels of short-wavelength UV (UVC) irradiation. The UVC-imposed global inhibition of the cellular translation machinery was significantly relieved after silencing of TIAR expression. We propose that the TIAR-mediated inhibition of translation factor expression elicits a sustained repression of protein biosynthesis in cells responding to stress.

scholarly journals The yeast transcription elongation factor Spt4/5 is a sequence-specific RNA binding protein

2016 ◽  
Vol 25 (9) ◽  
pp. 1710-1721 ◽  
Author(s):  
Amanda J. Blythe ◽  
Berra Yazar-Klosinski ◽  
Michael W. Webster ◽  
Eefei Chen ◽  
Marylène Vandevenne ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Transcription Elongation ◽  
Rna Binding Protein ◽  
Elongation Factor ◽  
Transcription Elongation Factor

scholarly journals A tail of translational regulation

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Gillian A Gray ◽  
Nicola K Gray
Keyword(s):  
Protein Synthesis ◽  
Translational Regulation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein

An RNA-binding protein called PABPC1 has an important role in determining protein synthesis rates and hypertrophy in the heart.

scholarly journals Effects of antibody to 5 S-RNA-binding protein on protein synthesis in Artemia salina ribosomes

1989 ◽  
Vol 259 (1) ◽  
pp. 277-281 ◽  
Author(s):  
N Kenmochi ◽  
Y Takahashi ◽  
N L Sato
Keyword(s):  
Protein Synthesis ◽  
Rna Binding ◽  
Rna Binding Protein ◽  
Elongation Factor ◽  
Artemia Salina ◽  
Globin Mrna ◽  
Ribosomal Subunits ◽  
Elongation Factor 2 ◽  
Subunit Interface

The effects of an affinity-purified polyclonal antibody to Artemia salina ribosomal protein L5 on protein synthesis in vitro were examined. The antibody interacted with 60 S subunits more strongly than with 80 S ribosomes, and inhibited reassociation of ribosomal subunits to some extent at 5 mM-Mg2+ but not at 10 mM. Polyphenylalanine synthesis in vitro at 10 mM-Mg2+ was significantly inhibited, especially when the antibody was first preincubated with 60 S subunits prior to the assay. The incorporation of amino acid directed by globin mRNA was inhibited only when the preincubation with 60 S subunits was carried out. On the other hand, no effect was detected on elongation factor 2- and 60 S subunit-dependent uncoupled GTPase activity. These results suggest that L5 is probably located at or near the subunit interface and may play an important role in protein synthesis.

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