Large Favorable Enthalpy Changes Drive Specific RNA Recognition by RNA Recognition Motif Proteins

The RNA recognition motif (RRM) is a prevalent class of RNA binding domains. Although a number of RRM/RNA structures have been determined, thermodynamic analyses are relatively uncommon. Here, we use isothermal titration calorimetry to characterize single-stranded (ss)RNA binding by four representat...

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Bibliographic Details
Published in:Biochemistry (Easton) 2011-03, Vol.50 (9), p.1429-1431
Main Authors: McLaughlin, Krystle J, Jenkins, Jermaine L, Kielkopf, Clara L
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Binding Sites
Mutation
Protein Binding
RNA - chemistry
RNA - metabolism
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
Thermodynamics
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Summary:The RNA recognition motif (RRM) is a prevalent class of RNA binding domains. Although a number of RRM/RNA structures have been determined, thermodynamic analyses are relatively uncommon. Here, we use isothermal titration calorimetry to characterize single-stranded (ss)RNA binding by four representative RRM-containing proteins: (i) U2AF65, (ii) SXL, (iii) TIA-1, and (iv) PAB. In all cases, ssRNA binding is accompanied by remarkably large favorable enthalpy changes (−30 to −60 kcal mol−1) and unfavorable entropy changes. Alterations of key RRM residues and binding sites indicate that under the nearly physiological conditions of these studies, large thermodynamic changes represent a signature of specific ssRNA recognition by RRMs.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi102057m