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====Adenosine Recognition via Hydrogen Bonding====
====Adenosine Recognition via Hydrogen Bonding====
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====Aromatic Stacking====
 
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== Function ==
 
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In eukaryotic mRNA translation, PABP recognizes the 3' Poly(A) tail via trough interactions determined above. While associated with the Poly(A) region, the complex then works together to stabilize the mRNA by preventing exoribonucleolytic degradation,¹ thereby guiding the mRNA molecule into the translation pathway via interactions with translation initiation factor gG.
 
- 
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===Recognition of the poly(A) tail===
 
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Polyadenylation of an mRNA involves the recognition of the 5’-AAUAAA-3’ consensus site, the cleavage downstream of the consensus site, and then the addition of adenines by [https://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase Poly(A) Polymerase] to the 3’ end. The newly added poly(A) tail is associated with the PABP. PABP requires 11-12 adenosines in order to bind. PABP and the bound Poly(A) tail work together to stabilize mRNA by preventing exo-ribonucleolytic degradation,¹ thereby guiding the mRNA molecule into the translation pathway. Upon mRNA poly(A) recognition, PABP and the bound mRNA stimulate the initiation of translation by interacting with initiation factor [https://en.wikipedia.org/wiki/EIF4G eIF4G]. Mutations of Arg→Ala and Lys→Ala in human eIF4G and in yeast extracts decrease the rate of translation initiation and destabilizing the interactions with PABP, indicating that basic residues are essential to the interaction with PABP.¹
 
<table><tr><td colspan='2'>
<table><tr><td colspan='2'>
<tr id='Adenosine Number'><td class="sblockLbl"><b>Adenosine Number</b></td><td class="sblockDat">PABP residue</td><td class="sblockDat">Atom on Protein</td>
<tr id='Adenosine Number'><td class="sblockLbl"><b>Adenosine Number</b></td><td class="sblockDat">PABP residue</td><td class="sblockDat">Atom on Protein</td>
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<tr id='A9'><td class="sblockLbl"><b>A9</b></td><td class="sblockDat"><scene name='78/782616/Arg44-a9/2'>Arginine 44</scene></td><td class="sblockDat">side chain τ-amine</td></tr>
<tr id='A9'><td class="sblockLbl"><b>A9</b></td><td class="sblockDat"><scene name='78/782616/Arg44-a9/2'>Arginine 44</scene></td><td class="sblockDat">side chain τ-amine</td></tr>
</table>
</table>
 +
====Aromatic Stacking====
 +
 +
== Function ==
 +
In eukaryotic mRNA translation, PABP recognizes the 3' Poly(A) tail via trough interactions determined above. While associated with the Poly(A) region, the complex then works together to stabilize the mRNA by preventing exoribonucleolytic degradation,¹ thereby guiding the mRNA molecule into the translation pathway via interactions with translation initiation factor gG.
 +
 +
===Recognition of the poly(A) tail===
 +
Polyadenylation of an mRNA involves the recognition of the 5’-AAUAAA-3’ consensus site, the cleavage downstream of the consensus site, and then the addition of adenines by [https://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase Poly(A) Polymerase] to the 3’ end. The newly added poly(A) tail is associated with the PABP. PABP requires 11-12 adenosines in order to bind. PABP and the bound Poly(A) tail work together to stabilize mRNA by preventing exo-ribonucleolytic degradation,¹ thereby guiding the mRNA molecule into the translation pathway. Upon mRNA poly(A) recognition, PABP and the bound mRNA stimulate the initiation of translation by interacting with initiation factor [https://en.wikipedia.org/wiki/EIF4G eIF4G]. Mutations of Arg→Ala and Lys→Ala in human eIF4G and in yeast extracts decrease the rate of translation initiation and destabilizing the interactions with PABP, indicating that basic residues are essential to the interaction with PABP.¹
 +

Revision as of 21:52, 2 April 2018

Human Poly(A) Binding Protein (1CVJ)

Caption for this structure

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References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

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David Ryskamp

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