Conserved thermochemistry of guanosine nucleophile binding for structurally distinct group I ribozymes.

Abstract:

:We report thermodynamic values for binding of the guanosine nucleophile to the ribozyme derived from the Anabaena group I intron, and find that they are similar to those measured previously for the structurally distinct Tetrahymena ribozyme. The free energy of binding guanosine 5'-monophosphate (pG) at 30 degrees C is similar for the two ribozymes. The delta(H)degrees' and delta(S)degrees' for pG binding to the Anabaena ribozyme--RNA substrate complex (E x S) are 3.4 +/- 4 kcal/mol and 27 +/- 10 e.u., respectively. The negligible enthalpic contribution and positive entropy change were found previously for the Tetrahymena ribozyme, and are considered remarkable for a hydrogen-bonding interaction between a nucleotide and a nucleic acid. These thermodynamic values may reflect conformational changes or water release upon pG binding that are comparable for the two ribozymes. In addition, the apparent chemical steps of the two ribozyme reactions share similar activation energies and a positive deltaS++. It now appears that such thermochemical values for guanosine binding and activation may be intrinsic properties of the group I intron catalytic center.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Kuo LY,Cech TR

doi

10.1093/nar/24.19.3722

subject

Has Abstract

pub_date

1996-10-01 00:00:00

pages

3722-7

issue

19

eissn

0305-1048

issn

1362-4962

pii

6t0335

journal_volume

24

pub_type

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