The HMGB1 C-Terminal Tail Regulates DNA Bending
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- 作者：Rebecca H. Blair&dagger ; ; 1 ; Abigail E. Horn&dagger ; ; Yogitha Pazhani ; Lizbeth Grado ; James A. Goodrich ; james.goodrich@colorado.edu" class="auth_mail" title="E-mail the corresponding author ; Jennifer F. Kugel ; jennifer.kugel@colorado.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：AB protein ; protein containing the HMGB1 A box and B box domains ; AB-F38A ; AB protein with a point mutation changing Phe38 to Ala ; BC ; protein containing the HMGB1 B box domain and C-terminal tail ; BSA ; Bovine serum albumin ; CCD ; charge-coupled device ; dsDNA ; double-stranded DNA ; EMSA ; electrophoretic mobility shift assay ; FL ; full-length ; FL-F38A ; FL HMGB1 with a point mutation changing Phe38 to Ala ; FRET ; fluorescence resonance energy transfer ; HMG ; high mobility group ; HMGB1 ; high mobility gr
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：9 October 2016
- 年：2016
- 卷：428
- 期：20
- 页码：4060-4072
- 全文大小：1139 K
文摘
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HMGB1 is a multidomain protein that binds and bends DNA non-sequence specifically.
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DNA bending by HMGB1 domains was monitored using single-molecule FRET.
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FL HMGB1 bent DNA slightly more than the A box and B box individually.
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Deleting the HMGB1 C-terminal tail caused DNA to be bent into a higher FRET state.
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Data support the model that the C-terminal tail impedes DNA binding by the B box.