The DNA-Binding High-Mobility Group Box Domain of Sox Family Proteins Directly Interacts with RNA In Vitro.
The DNA-Binding High-Mobility Group Box Domain of Sox Family Proteins Directly Interacts with RNA In Vitro.
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DOI:
10.1021/acs.biochem.2c00218
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发表时间:
2022-05-05
期刊:
影响因子:
2.9
通讯作者:
Batey, Robert T.
中科院分区:
文献类型:
--
作者:
Hamilton, Desmond J.;Hein, Abigail E.;Holmes, Zachariah E.;Wuttke, Deborah S.;Batey, Robert T.
There is growing evidence that a substantial number of protein domains ascribed as DNA-binding also interact with RNA to regulate biological processes. Several recent studies have revealed that the Sox2 transcription factor binds RNA through its high mobility group box (HMGB) domain in vitro and in vivo. High conservation of this domain amongst members of the Sox family of transcription factors suggests that RNA-binding activity may be a general feature of these proteins. To address this hypothesis, we examined a subset of HMGB domains from human Sox family proteins for their ability to bind both DNA and RNA in vitro. We observed selective, high affinity interactions between Sox family HMGB domains and various model RNA elements including a four-way junction RNA, a hairpin RNA with an internal bulge, G-quadruplex RNA, and a fragment of the long non-coding RNA ES2, which is known to directly interact with Sox2. Importantly, the HMGB domains bind these RNA ligands significantly tighter than non-consensus dsDNA and in some cases with affinities rivaling their consensus dsDNA sequences. These data suggest that RNA-binding is a conserved feature of the Sox family of transcription factors with the potential to modulate unappreciated biological functions.
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DOI:
10.1073/pnas.91.8.3368
发表时间:
1994-04-12
影响因子:
11.1
作者:
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通讯作者:
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影响因子:
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影响因子:
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作者:
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通讯作者:
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