Cooperation between bHLH transcription factors and histones for DNA access

被引:31
|
作者
Michael, Alicia K. [1 ,2 ]
Stoos, Lisa [1 ,2 ]
Crosby, Priya [3 ]
Eggers, Nikolas [4 ]
Nie, Xinyu Y. [5 ]
Makasheva, Kristina [6 ]
Minnich, Martina [7 ]
Healy, Kelly L. [8 ]
Weiss, Joscha [1 ,2 ]
Kempf, Georg [1 ]
Cavadini, Simone [1 ]
Kater, Lukas [1 ]
Seebacher, Jan [1 ]
Vecchia, Luca [1 ]
Chakraborty, Deyasini [1 ,2 ]
Isbel, Luke [1 ]
Grand, Ralph S. [1 ]
Andersch, Florian [7 ]
Fribourgh, Jennifer L. [3 ]
Schuebeler, Dirk [1 ,2 ]
Zuber, Johannes [7 ,9 ]
Liu, Andrew C. [8 ]
Becker, Peter B. [4 ]
Fierz, Beat [6 ]
Partch, Carrie L. [3 ]
Menet, Jerome S. [5 ]
Thomae, Nicolas H. [1 ]
机构
[1] Friedrich Miescher Inst Biomed Res, Basel, Switzerland
[2] Univ Basel, Basel, Switzerland
[3] Univ Calif Santa Cruz, Dept Chem & Biochem, Santa Cruz, CA USA
[4] Ludwig Maximilians Univ Munchen, Biomed Ctr, Mol Biol Div, Munich, Germany
[5] Texas A&M Univ, Ctr Biol Clock Res, Dept Biol, College Stn, TX USA
[6] Ecole Polytech Fed Lausanne, Inst Chem Sci & Engn, Lausanne, Switzerland
[7] Vienna Bioctr, Res Inst Mol Pathol, Vienna, Austria
[8] Univ Florida, Coll Med, Dept Physiol & Aging, Gainesville, FL USA
[9] Med Univ Vienna, Vienna, Austria
基金
欧盟地平线“2020”; 瑞士国家科学基金会; 美国国家卫生研究院; 欧洲研究理事会; 美国国家科学基金会;
关键词
CRYO-EM; CRYSTAL-STRUCTURE; CIRCADIAN CLOCK; DYNAMIC INTERACTIONS; PIONEER FACTORS; NUCLEOSOMES; CHROMATIN; BINDING; PARTICLE; COMPLEX;
D O I
10.1038/s41586-023-06282-3
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The basic helix-loop-helix (bHLH) family of transcription factors recognizes DNA motifs known as E-boxes (CANNTG) and includes 108 members(1). Here we investigate how chromatinized E-boxes are engaged by two structurally diverse bHLH proteins: the proto-oncogene MYC-MAX and the circadian transcription factor CLOCK-BMAL1 (refs. 2,3). Both transcription factors bind to E-boxes preferentially near the nucleosomal entry-exit sites. Structural studies with engineered or native nucleosome sequences show that MYC-MAX or CLOCK-BMAL1 triggers the release of DNA from histones to gain access. Atop the H2A-H2B acidic patch(4), the CLOCK-BMAL1 Per-Arnt-Sim (PAS) dimerization domains engage the histone octamer disc. Binding of tandem E-boxes(5-7) at endogenous DNA sequences occurs through direct interactions between two CLOCK-BMAL1 protomers and histones and is important for circadian cycling. At internal E-boxes, the MYC-MAX leucine zipper can also interact with histones H2B and H3, and its binding is indirectly enhanced by OCT4 elsewhere on the nucleosome. The nucleosomal E-box position and the type of bHLH dimerization domain jointly determine the histone contact, the affinity and the degree of competition and cooperativity with other nucleosome-bound factors.
引用
收藏
页码:385 / +
页数:42
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