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Biochemistry. 2011 Mar 8;50(9):1429-31. doi: 10.1021/bi102057m. Epub 2011 Feb 2.

Large favorable enthalpy changes drive specific RNA recognition by RNA recognition motif proteins.

Author information

1
Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642, United States.

Abstract

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) U2AF(65), (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.

PMID:
21261285
PMCID:
PMC3050080
DOI:
10.1021/bi102057m
[Indexed for MEDLINE]
Free PMC Article

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