Literature DB >> 8115165

Applicability of PM3 to transphosphorylation reaction path: toward designing a minimal ribozyme.

J I Manchester1, M Shibata, R F Setlik, R L Ornstein, R Rein.   

Abstract

A growing body of evidence shows that RNA can catalyze many of the reactions necessary both for replication of genetic material and the possible transition into the modern protein-based world. However, contemporary ribozymes are too large to have self-assembled from a prebiotic oligonucleotide pool. Still, it is likely that the major features of the earliest ribozymes have been preserved as molecular fossils in the catalytic RNA of today. Therefore, the search for a minimal ribozyme has been aimed at finding the necessary structural features of a modern ribozyme (Beaudry and Joyce, 1990). Both a three-dimensional model and quantum chemical calculations are required to quantitatively determine the effects of structural features of the ribozyme on the reaction it catalyzes. Using this model, quantum chemical calculations must be performed to determine quantitatively the effects of structural features on catalysis. Previous studies of the reaction path have been conducted at the ab initio level, but these methods are limited to small models due to enormous computational requirements. Semiempirical methods have been applied to large systems in the past; however, the accuracy of these methods depends largely on the system under investigation. In the present study we assess the validity of the MNDO/PM3 method on a simple model of the ribozyme-catalyzed reaction, or hydrolysis of phosphoric acid. We find that the results are qualitatively similar to ab initio results using large basis sets. Therefore, PM3 is suitable for studying the reaction path of the ribozyme-catalyzed reaction.

Entities:  

Keywords:  NASA Discipline Exobiology; Non-NASA Center

Mesh:

Substances:

Year:  1993        PMID: 8115165     DOI: 10.1007/bf01582089

Source DB:  PubMed          Journal:  Orig Life Evol Biosph        ISSN: 0169-6149            Impact factor:   1.950


  22 in total

1.  A molecular orbital study of a model of the Mg2+ coordination complex of the self splicing reaction of ribosomal RNA.

Authors:  M McCourt; M Shibata; J W McIver; R Rein
Journal:  J Mol Struct       Date:  1988       Impact factor: 3.196

2.  Oligomerization of ribonucleotides on montmorillonite: reaction of the 5'-phosphorimidazolide of adenosine.

Authors:  J P Ferris; G Ertem
Journal:  Science       Date:  1992-09-04       Impact factor: 47.728

3.  Minimum secondary structure requirements for catalytic activity of a self-splicing group I intron.

Authors:  A A Beaudry; G F Joyce
Journal:  Biochemistry       Date:  1990-07-10       Impact factor: 3.162

4.  Unusual resistance of peptidyl transferase to protein extraction procedures.

Authors:  H F Noller; V Hoffarth; L Zimniak
Journal:  Science       Date:  1992-06-05       Impact factor: 47.728

5.  A model for the RNA-catalyzed replication of RNA.

Authors:  T R Cech
Journal:  Proc Natl Acad Sci U S A       Date:  1986-06       Impact factor: 11.205

6.  The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme.

Authors:  C Guerrier-Takada; K Gardiner; T Marsh; N Pace; S Altman
Journal:  Cell       Date:  1983-12       Impact factor: 41.582

7.  Oligomerization reactions of ribonucleotides: the reaction of the 5'-phosphorimidazolide of nucleosides on montmorillonite and other minerals.

Authors:  J P Ferris; G Ertem
Journal:  Orig Life Evol Biosph       Date:  1992       Impact factor: 1.950

8.  Aminoacyl esterase activity of the Tetrahymena ribozyme.

Authors:  J A Piccirilli; T S McConnell; A J Zaug; H F Noller; T R Cech
Journal:  Science       Date:  1992-06-05       Impact factor: 47.728

9.  Theoretical analyses on the role of Mg2+ ions in ribozyme reactions.

Authors:  T Uchimaru; M Uebayasi; K Tanabe; K Taira
Journal:  FASEB J       Date:  1993-01       Impact factor: 5.191

10.  Catalytic activity of aminoacyl tRNA synthetases and its implications for the origin of life. I. Aminoacyl adenylate formation in tyrosyl tRNA synthetase.

Authors:  W A Sokalski; M Shibata; D Barak; R Rein
Journal:  J Mol Evol       Date:  1991-11       Impact factor: 2.395

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