Regulation of transcription attenuation and translation initiation by allosteric control of an RNA-binding protein: the Bacillus subtilis TRAP protein

2004 ◽  
Vol 7 (2) ◽  
pp. 132-139 ◽  
Author(s):  
Paul Babitzke
Keyword(s):  
Bacillus Subtilis ◽  
Translation Initiation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Regulation Of Transcription ◽  
Allosteric Control ◽  
Transcription Attenuation

Polypyrimidine-tract-binding protein: a multifunctional RNA-binding protein

2008 ◽  
Vol 36 (4) ◽  
pp. 641-647 ◽  
Author(s):  
Kirsty Sawicka ◽  
Martin Bushell ◽  
Keith A. Spriggs ◽  
Anne E. Willis
Keyword(s):  
Translation Initiation ◽  
Cellular Localization ◽  
Rna Binding ◽  
Binding Protein ◽  
Control Cell ◽  
Rna Binding Protein ◽  
Alternative Form ◽  
Polypyrimidine Tract ◽  
Polypyrimidine Tract Binding ◽  
Polypyrimidine Tract Binding Protein

PTB (polypyrimidine-tract-binding protein) is a ubiquitous RNA-binding protein. It was originally identified as a protein with a role in splicing but it is now known to function in a large number of diverse cellular processes including polyadenylation, mRNA stability and translation initiation. Specificity of PTB function is achieved by a combination of changes in the cellular localization of this protein (its ability to shuttle from the nucleus to the cytoplasm is tightly controlled) and its interaction with additional proteins. These differences in location and trans-acting factor requirements account for the fact that PTB acts both as a suppressor of splicing and an activator of translation. In the latter case, the role of PTB in translation has been studied extensively and it appears that this protein is required for an alternative form of translation initiation that is mediated by a large RNA structural element termed an IRES (internal ribosome entry site) that allows the synthesis of picornaviral proteins and cellular proteins that function to control cell growth and cell death. In the present review, we discuss how PTB regulates these disparate processes.

scholarly journals Regulation of transcription factor MEF2C by RNA binding protein HuR

2017 ◽  
Vol 2 (5) ◽  
pp. 210
Author(s):  
Z. Anyu ◽  
G. Shi ◽  
A. Xie ◽  
D. Aksoy ◽  
S. Dudley
Keyword(s):  
Transcription Factor ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Regulation Of Transcription

scholarly journals Neural RNA-binding protein Musashi1 inhibits translation initiation by competing with eIF4G for PABP

2008 ◽  
Vol 181 (4) ◽  
pp. 639-653 ◽  
Author(s):  
Hironori Kawahara ◽  
Takao Imai ◽  
Hiroaki Imataka ◽  
Masafumi Tsujimoto ◽  
Ken Matsumoto ◽  
...  
Keyword(s):  
Stem Cells ◽  
Neural Stem Cells ◽  
Translation Initiation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Stress Granules ◽  
Translational Repression ◽  
Rna Recognition Motifs ◽  
Recognition Motifs

Musashi1 (Msi1) is an RNA-binding protein that is highly expressed in neural stem cells. We previously reported that Msi1 contributes to the maintenance of the immature state and self-renewal activity of neural stem cells through translational repression of m-Numb. However, its translation repression mechanism has remained unclear. Here, we identify poly(A) binding protein (PABP) as an Msi1-binding protein, and find Msi1 competes with eIF4G for PABP binding. This competition inhibits translation initiation of Msi1's target mRNA. Indeed, deletion of the PABP-interacting domain in Msi1 abolishes its function. We demonstrate that Msi1 inhibits the assembly of the 80S, but not the 48S, ribosome complex. Consistent with these conclusions, Msi1 colocalizes with PABP and is recruited into stress granules, which contain the stalled preinitiation complex. However, Msi1 with mutations in two RNA recognition motifs fails to accumulate into stress granules. These results provide insight into the mechanism by which sequence-specific translational repression occurs in stem cells through the control of translation initiation.

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