FEBS Letters | |
The DNA recognition subunit of a DNA methyltransferase is predominantly a molten globule in the absence of DNA | |
Price, Nicholas C.1  Waltho, Jonathan2  Hornby, David P.2  Shore, Paul2  Whitmarsh, Alan2  Baldwin, Geoffrey S.2  Kelly, Sharon M.1  Pinarbasi, Hatice2  | |
[1] Department of Biological and Molecular Sciences, University of Stirling, Stirling, FK9 4LA, Scotland, UK;Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, UK | |
关键词: DNA methylase; Molten globule; Binding specificity; Nuclear magnetic resonance; Circular dichroism; C5 MTase; cytosine (C5)-specific DNA methyltransferase; NMR; nuclear magnetic resonance; CD; circular dichroism; AdoMet; S-adenosyl methionine; ANS 1-anilinonaphthalene-8-sulphonate; TRD; target recognition domain; | |
DOI : 10.1016/0014-5793(94)01171-0 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Enzyme-catalysed DNA methylation provides an opportunity for the modulation of protein-DNA recognition in biological systems. Recently we have demonstrated that the smaller of the two subunits of the heterodimeric, cytosine-specific DNA methyltransferase, M.AquI, is largely responsible for sequence-specific DNA recognition. Here we present evidence from a series of NMR, fluorescence and circular dichroism spectroscopy experiments that the DNA binding subunit of M.AquI has the characteristics of a molten globule in the absence of the catalytic machinery. In this metastable state this subunit retains its ability to bind DNA in a sequence-specific manner. We believe this finding offers an insight into the structural flexibility which underpins the mechansim of action of these enzymes, and may provide a possible biological role for molten globules in protein function.
【 授权许可】
Unknown
【 预 览 】
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