Literature DB >> 17028142

Mechanical unfolding of RNA: from hairpins to structures with internal multiloops.

Changbong Hyeon1, D Thirumalai.   

Abstract

Mechanical unfolding of RNA structures, ranging from hairpins to ribozymes, using laser optical tweezer experiments have begun to reveal the features of the energy landscape that cannot be easily explored using conventional experiments. Upon application of constant force (f), RNA hairpins undergo cooperative transitions from folded to unfolded states whereas subdomains of ribozymes unravel one at a time. Here, we use a self-organized polymer model and Brownian dynamics simulations to probe mechanical unfolding at constant force and constant-loading rate of four RNA structures of varying complexity. For simple hairpins, such as P5GA, application of constant force or constant loading rate results in bistable cooperative transitions between folded and unfolded states without populating any intermediates. The transition state location (DeltaxFTS) changes dramatically as the loading rate is varied. At loading rates comparable to those used in laser optical tweezer experiments, the hairpin is plastic, with DeltaxFTS being midway between folded and unfolded states; whereas at high loading rates, DeltaxFTS moves close to the folded state, i.e., RNA is brittle. For the 29-nucleotide TAR RNA with the three-nucleotide bulge, unfolding occurs in a nearly two-state manner with an occasional pause in a high free energy metastable state. Forced unfolding of the 55 nucleotides of the Hepatitis IRES domain IIa, which has a distorted L-shaped structure, results in well-populated stable intermediates. The most stable force-stabilized intermediate represents straightening of the L-shaped structure. For these structures, the unfolding pathways can be predicted using the contact map of the native structures. Unfolding of a RNA motif with internal multiloop, namely, the 109-nucleotide prohead RNA that is part of the 29 DNA packaging motor, at constant value of rf occurs with three distinct rips that represent unraveling of the paired helices. The rips represent kinetic barriers to unfolding. Our work shows 1), the response of RNA to force is largely determined by the native structure; and 2), only by probing mechanical unfolding over a wide range of forces can the underlying energy landscape be fully explored.

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Year:  2006        PMID: 17028142      PMCID: PMC1779982          DOI: 10.1529/biophysj.106.093062

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  38 in total

1.  Structure of the bacteriophage phi29 DNA packaging motor.

Authors:  A A Simpson; Y Tao; P G Leiman; M O Badasso; Y He; P J Jardine; N H Olson; M C Morais; S Grimes; D L Anderson; T S Baker; M G Rossmann
Journal:  Nature       Date:  2000-12-07       Impact factor: 49.962

2.  Reversible unfolding of single RNA molecules by mechanical force.

Authors:  J Liphardt; B Onoa; S B Smith; I Tinoco; C Bustamante
Journal:  Science       Date:  2001-04-27       Impact factor: 47.728

3.  Native topology determines force-induced unfolding pathways in globular proteins.

Authors:  D K Klimov; D Thirumalai
Journal:  Proc Natl Acad Sci U S A       Date:  2000-06-20       Impact factor: 11.205

4.  Force-induced denaturation of RNA.

Authors:  U Gerland; R Bundschuh; T Hwa
Journal:  Biophys J       Date:  2001-09       Impact factor: 4.033

Review 5.  Beyond kinetic traps in RNA folding.

Authors:  D K Treiber; J R Williamson
Journal:  Curr Opin Struct Biol       Date:  2001-06       Impact factor: 6.809

6.  Solution structure of Cobalt(III)hexammine complexed to the GAAA tetraloop, and metal-ion binding to G.A mismatches.

Authors:  S Rüdisser; I Tinoco
Journal:  J Mol Biol       Date:  2000-02-04       Impact factor: 5.469

Review 7.  The chemical repertoire of natural ribozymes.

Authors:  Jennifer A Doudna; Thomas R Cech
Journal:  Nature       Date:  2002-07-11       Impact factor: 49.962

8.  Equilibrium information from nonequilibrium measurements in an experimental test of Jarzynski's equality.

Authors:  Jan Liphardt; Sophie Dumont; Steven B Smith; Ignacio Tinoco; Carlos Bustamante
Journal:  Science       Date:  2002-06-07       Impact factor: 47.728

9.  Pathways and kinetic barriers in mechanical unfolding and refolding of RNA and proteins.

Authors:  Changbong Hyeon; Ruxandra I Dima; D Thirumalai
Journal:  Structure       Date:  2006-11       Impact factor: 5.006

10.  Identifying kinetic barriers to mechanical unfolding of the T. thermophila ribozyme.

Authors:  Bibiana Onoa; Sophie Dumont; Jan Liphardt; Steven B Smith; Ignacio Tinoco; Carlos Bustamante
Journal:  Science       Date:  2003-03-21       Impact factor: 47.728

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  37 in total

1.  Compaction and tensile forces determine the accuracy of folding landscape parameters from single molecule pulling experiments.

Authors:  Greg Morrison; Changbong Hyeon; Michael Hinczewski; D Thirumalai
Journal:  Phys Rev Lett       Date:  2011-03-29       Impact factor: 9.161

Review 2.  Taming free energy landscapes with RNA chaperones.

Authors:  Sarah A Woodson
Journal:  RNA Biol       Date:  2010-11-01       Impact factor: 4.652

3.  Computing the conformational entropy for RNA folds.

Authors:  Liang Liu; Shi-Jie Chen
Journal:  J Chem Phys       Date:  2010-06-21       Impact factor: 3.488

4.  Promoter melting triggered by bacterial RNA polymerase occurs in three steps.

Authors:  Jie Chen; Seth A Darst; D Thirumalai
Journal:  Proc Natl Acad Sci U S A       Date:  2010-07-01       Impact factor: 11.205

5.  Targeted binding of nucleocapsid protein transforms the folding landscape of HIV-1 TAR RNA.

Authors:  Micah J McCauley; Ioulia Rouzina; Kelly A Manthei; Robert J Gorelick; Karin Musier-Forsyth; Mark C Williams
Journal:  Proc Natl Acad Sci U S A       Date:  2015-10-19       Impact factor: 11.205

6.  Using simulations and kinetic network models to reveal the dynamics and functions of riboswitches.

Authors:  Jong-Chin Lin; Jeseong Yoon; Changbong Hyeon; D Thirumalai
Journal:  Methods Enzymol       Date:  2015-02-03       Impact factor: 1.600

7.  Internal strain regulates the nucleotide binding site of the kinesin leading head.

Authors:  Changbong Hyeon; José N Onuchic
Journal:  Proc Natl Acad Sci U S A       Date:  2007-02-07       Impact factor: 11.205

8.  Coarse-grained free energy functions for studying protein conformational changes: a double-well network model.

Authors:  Jhih-Wei Chu; Gregory A Voth
Journal:  Biophys J       Date:  2007-08-17       Impact factor: 4.033

9.  A new computational approach for mechanical folding kinetics of RNA hairpins.

Authors:  Song Cao; Shi-Jie Chen
Journal:  Biophys J       Date:  2009-05-20       Impact factor: 4.033

10.  Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition.

Authors:  Jie Chen; D Thirumalai
Journal:  Biochemistry       Date:  2012-12-31       Impact factor: 3.162

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