Role of protein-protein interactions on organization and dynamics of a model chromatin

被引:2
作者
Swain, Pinaki [1 ,2 ]
Choubey, Sandeep [1 ,2 ]
Vemparala, Satyavani [1 ,2 ]
机构
[1] Inst Math Sci, CIT Campus, Chennai 600113, India
[2] Homi Bhabha Natl Inst, Training Sch Complex, Mumbai 400094, India
关键词
MICROPHASE SEPARATION; PHASE-SEPARATION; REVEALS; MECHANISMS; PRINCIPLES; COMPACTION; DOMAINS; MOTION; YEAST;
D O I
10.1063/5.0222708
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The three-dimensional organization of chromatin is influenced by chromatin-binding proteins through both specific and non-specific interactions. However, the roles of chromatin sequence and the interactions between binding proteins in shaping chromatin structure remain elusive. By employing a simple polymer-based model of chromatin that explicitly considers sequence-dependent protein binding and protein-protein interactions, we elucidate a mechanism for chromatin organization. We find that tuning protein-protein interactions and protein concentration is sufficient to either promote or inhibit chromatin compartmentalization. Moreover, chromatin sequence and protein-protein attraction strongly affect the structural and dynamic exponents that describe the spatiotemporal organization of chromatin. Strikingly, our model's predictions for the exponents governing chromatin structure and dynamics successfully capture experimental observations, in sharp contrast to previous chromatin models. Overall, our findings have the potential to reinterpret data obtained from various chromosome conformation capture technologies, laying the groundwork for advancing our understanding of chromatin organization.
引用
收藏
页数:14
相关论文
共 88 条
[1]  
Adame-Arana Omar, 2023, Elife, V12, DOI 10.7554/eLife.82983
[2]   Simulating the chromatin-mediated phase separation of model proteins with multiple domains [J].
Ancona, Marco ;
Brackley, Chris A. .
BIOPHYSICAL JOURNAL, 2022, 121 (13) :2600-2612
[3]  
Bajpai G, 2020, BIOPHYS J, V118, p549A
[4]   Complexity of chromatin folding is captured by the strings and binders switch model [J].
Barbieri, Mariano ;
Chotalia, Mita ;
Fraser, James ;
Lavitas, Liron-Mark ;
Dostie, Josee ;
Pombo, Ana ;
Nicodemi, Mario .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2012, 109 (40) :16173-16178
[5]   Super-resolution chromatin tracing reveals domains and cooperative interactions in single cells [J].
Bintu, Bogdan ;
Mateo, Leslie J. ;
Su, Jun-Han ;
Sinnott-Armstrong, Nicholas A. ;
Parker, Mirae ;
Kinrot, Seon ;
Yamaya, Kei ;
Boettiger, Alistair N. ;
Zhuang, Xiaowei .
SCIENCE, 2018, 362 (6413) :419-+
[6]   Super-resolution imaging reveals distinct chromatin folding for different epigenetic states [J].
Boettiger, Alistair N. ;
Bintu, Bogdan ;
Moffitt, Jeffrey R. ;
Wang, Siyuan ;
Beliveau, Brian J. ;
Fudenberg, Geoffrey ;
Imakaev, Maxim ;
Mirny, Leonid A. ;
Wu, Chao-ting ;
Zhuang, Xiaowei .
NATURE, 2016, 529 (7586) :418-+
[7]   Nonequilibrium Chromosome Looping via Molecular Slip Links [J].
Brackley, C. A. ;
Johnson, J. ;
Michieletto, D. ;
Morozov, A. N. ;
Nicodemi, M. ;
Cook, P. R. ;
Marenduzzo, D. .
PHYSICAL REVIEW LETTERS, 2017, 119 (13)
[8]   Predicting the three-dimensional folding of cis-regulatory regions in mammalian genomes using bioinformatic data and polymer models [J].
Brackley, Chris A. ;
Brown, Jill M. ;
Waithe, Dominic ;
Babbs, Christian ;
Davies, James ;
Hughes, Jim R. ;
Buckle, Veronica J. ;
Marenduzzo, Davide .
GENOME BIOLOGY, 2016, 17 :59
[9]   Nonspecific bridging-induced attraction drives clustering of DNA-binding proteins and genome organization [J].
Brackley, Chris A. ;
Taylor, Stephen ;
Papantonis, Argyris ;
Cook, Peter R. ;
Marenduzzo, Davide .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2013, 110 (38) :E3605-E3611
[10]   Exploring chromatin organization mechanisms through its dynamic properties [J].
Bronshtein, Irena ;
Kanter, Itamar ;
Kepten, Eldad ;
Lindner, Moshe ;
Berezin, Shirly ;
Shav-Tal, Yaron ;
Garini, Yuval .
NUCLEUS, 2016, 7 (01) :27-33