Literature DB >> 8159754

Kinetics of an RNA conformational switch.

K A LeCuyer1, D M Crothers.   

Abstract

The spliced leader RNA from Leptomonas collosoma has two competing secondary structures of nearly equal free energy. Short, complementary oligonucleotides can drive the structure from one form of the other. We report stopped-flow rapid-mixing and temperature-jump measurements of the kinetics of the structural switch. At high concentrations of oligonucleotide, the rate of binding becomes limited by the rate of the structural switch, which occurs on a time scale of a fraction of a second. The low activation energy observed for the process implies a branch migration type of mechanism in which portions of the two competing helices transiently coexist.

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Year:  1994        PMID: 8159754      PMCID: PMC43579          DOI: 10.1073/pnas.91.8.3373

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  18 in total

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Authors:  J A Steitz
Journal:  Science       Date:  1992-08-14       Impact factor: 47.728

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Authors:  H D Madhani; C Guthrie
Journal:  Cell       Date:  1992-11-27       Impact factor: 41.582

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Authors:  I G Wool; A Glück; Y Endo
Journal:  Trends Biochem Sci       Date:  1992-07       Impact factor: 13.807

4.  Permeable trypanosome cells as a model system for transcription and trans-splicing.

Authors:  E Ullu; C Tschudi
Journal:  Nucleic Acids Res       Date:  1990-06-11       Impact factor: 16.971

5.  Conformational changes of transfer ribonucleic acid. Relaxation kinetics of the early melting transition of methionine transfer ribonucleic acid (Escherichia coli).

Authors:  P E Cole; D M Crothers
Journal:  Biochemistry       Date:  1972-11-07       Impact factor: 3.162

6.  Relaxation kinetics of dimer formation by self complementary oligonucleotides.

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Journal:  J Mol Biol       Date:  1971-12-14       Impact factor: 5.469

7.  THE KINETICS OF DOUBLE HELIX FORMATION FROM POLYRIBOADENYLIC ACID AND POLYRIBOURIDYLIC ACID.

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Journal:  J Mol Biol       Date:  1971-12-14       Impact factor: 5.469

9.  Dynamics of ribozyme binding of substrate revealed by fluorescence-detected stopped-flow methods.

Authors:  P C Bevilacqua; R Kierzek; K A Johnson; D H Turner
Journal:  Science       Date:  1992-11-20       Impact factor: 47.728

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  28 in total

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