Nucleobase catalysis in ribozyme mechanism

Philip C. Bevilacqua, Rieko Yajima

Research output: Contribution to journalReview article

89 Citations (Scopus)

Abstract

RNA performs a wide range of functions in biology including catalysis of chemical reactions. A major goal in the field of ribozyme chemical biology is to understand these functions in molecular terms. There is increasing evidence that ribozymes can use their nucleobases directly in chemical catalysis in a variety of ways. These include hydrogen bonding to the transition state, stabilizing charge development, and transferring protons as general acid-base catalysts. This article highlights recent kinetic, structural, single molecule, and synthetic approaches that have been used to probe the roles of ribozyme nucleobases in phosphodiester bond cleavage.

Original languageEnglish (US)
Pages (from-to)455-464
Number of pages10
JournalCurrent Opinion in Chemical Biology
Volume10
Issue number5
DOIs
StatePublished - Oct 1 2006

Fingerprint

Catalytic RNA
Catalysis
Hydrogen Bonding
Protons
Chemical reactions
Hydrogen bonds
RNA
Catalysts
Molecules
Kinetics
Acids

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Biochemistry

Cite this

@article{cd247db5e0d345b58f6bdd0839164c38,
title = "Nucleobase catalysis in ribozyme mechanism",
abstract = "RNA performs a wide range of functions in biology including catalysis of chemical reactions. A major goal in the field of ribozyme chemical biology is to understand these functions in molecular terms. There is increasing evidence that ribozymes can use their nucleobases directly in chemical catalysis in a variety of ways. These include hydrogen bonding to the transition state, stabilizing charge development, and transferring protons as general acid-base catalysts. This article highlights recent kinetic, structural, single molecule, and synthetic approaches that have been used to probe the roles of ribozyme nucleobases in phosphodiester bond cleavage.",
author = "Bevilacqua, {Philip C.} and Rieko Yajima",
year = "2006",
month = "10",
day = "1",
doi = "10.1016/j.cbpa.2006.08.014",
language = "English (US)",
volume = "10",
pages = "455--464",
journal = "Current Opinion in Chemical Biology",
issn = "1367-5931",
publisher = "Elsevier Limited",
number = "5",

}

Nucleobase catalysis in ribozyme mechanism. / Bevilacqua, Philip C.; Yajima, Rieko.

In: Current Opinion in Chemical Biology, Vol. 10, No. 5, 01.10.2006, p. 455-464.

Research output: Contribution to journalReview article

TY - JOUR

T1 - Nucleobase catalysis in ribozyme mechanism

AU - Bevilacqua, Philip C.

AU - Yajima, Rieko

PY - 2006/10/1

Y1 - 2006/10/1

N2 - RNA performs a wide range of functions in biology including catalysis of chemical reactions. A major goal in the field of ribozyme chemical biology is to understand these functions in molecular terms. There is increasing evidence that ribozymes can use their nucleobases directly in chemical catalysis in a variety of ways. These include hydrogen bonding to the transition state, stabilizing charge development, and transferring protons as general acid-base catalysts. This article highlights recent kinetic, structural, single molecule, and synthetic approaches that have been used to probe the roles of ribozyme nucleobases in phosphodiester bond cleavage.

AB - RNA performs a wide range of functions in biology including catalysis of chemical reactions. A major goal in the field of ribozyme chemical biology is to understand these functions in molecular terms. There is increasing evidence that ribozymes can use their nucleobases directly in chemical catalysis in a variety of ways. These include hydrogen bonding to the transition state, stabilizing charge development, and transferring protons as general acid-base catalysts. This article highlights recent kinetic, structural, single molecule, and synthetic approaches that have been used to probe the roles of ribozyme nucleobases in phosphodiester bond cleavage.

UR - http://www.scopus.com/inward/record.url?scp=33748559498&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33748559498&partnerID=8YFLogxK

U2 - 10.1016/j.cbpa.2006.08.014

DO - 10.1016/j.cbpa.2006.08.014

M3 - Review article

VL - 10

SP - 455

EP - 464

JO - Current Opinion in Chemical Biology

JF - Current Opinion in Chemical Biology

SN - 1367-5931

IS - 5

ER -