Abstract
In most cases aminoacyl-tRNA synthetases (aaRSs) are negatively charged, as are the tRNA substrates. It is apparent that there are driving forces that provide a long-range attraction between like charge aaRS and tRNA, and ensure formation of "close encounters." Based on numerical solutions to the nonlinear Poisson-Boltzmann equation, we evaluated the electrostatic potential generated by different aaRSs. The 3D-isopotential surfaces calculated for different aaRSs at 0.01 kT/e contour level reveal the presence of large positive patches - one patch for each tRNA molecule. This is true for classes I and II monomers, dimers, and heterotetramers. The potential maps keep their characteristic features over a wide range of contour levels. The results suggest that nonspecific electrostatic interactions are the driving forces of primary stickiness of aaRSs-tRNA complexes. The long-range attraction in aaRS-tRNA systems is explained by capture of negatively charged tRNA into "blue space area" of the positive potential generated by aaRSs. Localization of tRNA in this area is a prerequisite for overcoming the barrier of Brownian motion.
Original language | English |
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Pages (from-to) | 1247-1251 |
Number of pages | 5 |
Journal | Protein Science |
Volume | 12 |
Issue number | 6 |
DOIs | |
State | Published - 1 Jun 2003 |
Externally published | Yes |
Keywords
- Aminoacyl-tRNA synthetase
- Brownian motion
- Electrostatic interactions
- Electrostatic potential
- Encounter complex
- tRNA