Large Favorable Enthalpy Changes Drive Specific RNA Recognition by RNA Recognition Motif Proteins
Large Favorable Enthalpy Changes Drive Specific RNA Recognition by RNA Recognition Motif Proteins
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DOI:
10.1021/bi102057m
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发表时间:
2011-03-08
期刊:
影响因子:
2.9
通讯作者:
Kielkopf, Clara L.
中科院分区:
文献类型:
--
作者:
McLaughlin, Krystle J.;Jenkins, Jermaine L.;Kielkopf, Clara L.
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.