Measuring DNA mechanics on the genome scale.


Journal

Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462

Informations de publication

Date de publication:
01 2021
Historique:
received: 11 04 2020
accepted: 21 10 2020
pubmed: 18 12 2020
medline: 27 2 2021
entrez: 17 12 2020
Statut: ppublish

Résumé

Mechanical deformations of DNA such as bending are ubiquitous and have been implicated in diverse cellular functions

Identifiants

pubmed: 33328628
doi: 10.1038/s41586-020-03052-3
pii: 10.1038/s41586-020-03052-3
pmc: PMC7855230
mid: NIHMS1640017
doi:

Substances chimiques

Codon 0
DNA, Fungal 0
INO80 complex, S cerevisiae 0
Nucleosomes 0
Saccharomyces cerevisiae Proteins 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

462-467

Subventions

Organisme : NIH HHS
ID : GM122569
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM130393
Pays : United States
Organisme : European Research Council
ID : 833613
Pays : International
Organisme : NIGMS NIH HHS
ID : R35 GM122569
Pays : United States
Organisme : Howard Hughes Medical Institute
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA163336
Pays : United States

Commentaires et corrections

Type : CommentIn
Type : CommentIn
Type : CommentIn

Références

Garcia, H. G. et al. Biological consequences of tightly bent DNA: the other life of a macromolecular celebrity. Biopolymers 85, 115–130 (2007).
doi: 10.1002/bip.20627
Krietenstein, N. et al. Genomic nucleosome organization reconstituted with pure proteins. Cell 167, 709–721 (2016).
doi: 10.1016/j.cell.2016.09.045
Shore, D., Langowski, J. & Baldwin, R. L. DNA flexibility studied by covalent closure of short fragments into circles. Proc. Natl Acad. Sci. USA 78, 4833–4837 (1981).
doi: 10.1073/pnas.78.8.4833
Cloutier, T. E. & Widom, J. Spontaneous sharp bending of double-stranded DNA. Mol. Cell 14, 355–362 (2004).
doi: 10.1016/S1097-2765(04)00210-2
Ha, T. et al. Probing the interaction between two single molecules: fluorescence resonance energy transfer between a single donor and a single acceptor. Proc. Natl Acad. Sci. USA 93, 6264–6268 (1996).
doi: 10.1073/pnas.93.13.6264
Vafabakhsh, R. & Ha, T. Extreme bendability of DNA less than 100 base pairs long revealed by single-molecule cyclization. Science 337, 1097–1101 (2012).
doi: 10.1126/science.1224139
Geggier, S. & Vologodskii, A. Sequence dependence of DNA bending rigidity. Proc. Natl Acad. Sci. USA 107, 15421–15426 (2010).
doi: 10.1073/pnas.1004809107
Beutel, B. A. & Gold, L. In vitro evolution of intrinsically bent DNA. J. Mol. Biol. 228, 803–812 (1992).
doi: 10.1016/0022-2836(92)90865-H
Rosanio, G., Widom, J. & Uhlenbeck, O. C. In vitro selection of DNAs with an increased propensity to form small circles. Biopolymers 103, 303–320 (2015).
doi: 10.1002/bip.22608
Jeong, J. & Kim, H. D. Base-pair mismatch can destabilize small DNA loops through cooperative kinking. Phys. Rev. Lett. 122, 218101 (2019).
doi: 10.1103/PhysRevLett.122.218101
Jeong, J. & Kim, H. D. Determinants of cyclization-decyclization kinetics of short DNA with sticky ends. Nucleic Acids Res. 48, 5147–5156 (2020).
doi: 10.1093/nar/gkaa207
Lee, W. et al. A high-resolution atlas of nucleosome occupancy in yeast. Nat. Genet. 39, 1235–1244 (2007).
doi: 10.1038/ng2117
Bai, L., Ondracka, A. & Cross, F. R. Multiple sequence-specific factors generate the nucleosome-depleted region on CLN2 promoter. Mol. Cell 42, 465–476 (2011).
doi: 10.1016/j.molcel.2011.03.028
Zhang, Z. et al. A packing mechanism for nucleosome organization reconstituted across a eukaryotic genome. Science 332, 977–980 (2011).
doi: 10.1126/science.1200508
Segal, E. & Widom, J. Poly(dA:dT) tracts: major determinants of nucleosome organization. Curr. Opin. Struct. Biol. 19, 65–71 (2009).
doi: 10.1016/j.sbi.2009.01.004
Segal, E. et al. A genomic code for nucleosome positioning. Nature 442, 772–778 (2006).
doi: 10.1038/nature04979
Chereji, R. V., Ramachandran, S., Bryson, T. D. & Henikoff, S. Precise genome-wide mapping of single nucleosomes and linkers in vivo. Genome Biol. 19, 19 (2018).
doi: 10.1186/s13059-018-1398-0
Gilchrist, D. A. et al. Pausing of RNA polymerase II disrupts DNA-specified nucleosome organization to enable precise gene regulation. Cell 143, 540–551 (2010).
doi: 10.1016/j.cell.2010.10.004
Zhou, C. Y. et al. The yeast INO80 complex operates as a tunable DNA length-sensitive switch to regulate nucleosome sliding. Mol. Cell 69, 677–688.e9 (2018).
doi: 10.1016/j.molcel.2018.01.028
Brahma, S. et al. INO80 exchanges H2A.Z for H2A by translocating on DNA proximal to histone dimers. Nat. Commun. 8, 15616 (2017).
doi: 10.1038/ncomms15616
Eustermann, S. et al. Structural basis for ATP-dependent chromatin remodelling by the INO80 complex. Nature 556, 386–390 (2018).
doi: 10.1038/s41586-018-0029-y
Brahma, S., Ngubo, M., Paul, S., Udugama, M. & Bartholomew, B. The Arp8 and Arp4 module acts as a DNA sensor controlling INO80 chromatin remodeling. Nat. Commun. 9, 3309 (2018).
doi: 10.1038/s41467-018-05710-7
Knoll, K. R. et al. The nuclear actin-containing Arp8 module is a linker DNA sensor driving INO80 chromatin remodeling. Nat. Struct. Mol. Biol. 25, 823–832 (2018).
doi: 10.1038/s41594-018-0115-8
Oberbeckmann, E. et al. Genome information processing by the INO80 chromatin remodeler positions nucleosomes. Preprint at https://doi.org/10.1101/2020.11.03.366690 (2020).
Kubik, S. et al. Nucleosome stability distinguishes two different promoter types at all protein-coding genes in yeast. Mol. Cell 60, 422–434 (2015).
doi: 10.1016/j.molcel.2015.10.002
Widom, J. Role of DNA sequence in nucleosome stability and dynamics. Q. Rev. Biophys. 34, 269–324 (2001).
doi: 10.1017/S0033583501003699
Drew, H. R. & Travers, A. A. DNA bending and its relation to nucleosome positioning. J. Mol. Biol. 186, 773–790 (1985).
doi: 10.1016/0022-2836(85)90396-1
Hayes, J. J., Tullius, T. D. & Wolffe, A. P. The structure of DNA in a nucleosome. Proc. Natl Acad. Sci. USA 87, 7405–7409 (1990).
doi: 10.1073/pnas.87.19.7405
Widlund, H. R. et al. Nucleosome structural features and intrinsic properties of the TATAAACGCC repeat sequence. J. Biol. Chem. 274, 31847–31852 (1999).
doi: 10.1074/jbc.274.45.31847
Shrader, T. E. & Crothers, D. M. Artificial nucleosome positioning sequences. Proc. Natl Acad. Sci. USA 86, 7418–7422 (1989).
doi: 10.1073/pnas.86.19.7418
Lowary, P. T. & Widom, J. New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning. J. Mol. Biol. 276, 19–42 (1998).
doi: 10.1006/jmbi.1997.1494
Jin, H., Rube, H. T. & Song, J. S. Categorical spectral analysis of periodicity in nucleosomal DNA. Nucleic Acids Res. 44, 2047–2057 (2016).
doi: 10.1093/nar/gkw101
Brogaard, K., Xi, L., Wang, J.-P. & Widom, J. A map of nucleosome positions in yeast at base-pair resolution. Nature 486, 496–501 (2012).
doi: 10.1038/nature11142
Ngo, T. T. M., Zhang, Q., Zhou, R., Yodh, J. G. & Ha, T. Asymmetric unwrapping of nucleosomes under tension directed by DNA local flexibility. Cell 160, 1135–1144 (2015).
doi: 10.1016/j.cell.2015.02.001
Bondarenko, V. A. et al. Nucleosomes can form a polar barrier to transcript elongation by RNA polymerase II. Mol. Cell 24, 469–479 (2006).
doi: 10.1016/j.molcel.2006.09.009
Nakano, M. et al. Single-molecule PCR using water-in-oil emulsion. J. Biotechnol. 102, 117–124 (2003).
doi: 10.1016/S0168-1656(03)00023-3
Langmead, B., Trapnell, C., Pop, M. & Salzberg, S. L. Ultrafast and memory-efficient alignment of short DNA sequences to the human genome. Genome Biol. 10, R25 (2009).
doi: 10.1186/gb-2009-10-3-r25
Li, H. et al. The Sequence Alignment/Map format and SAMtools. Bioinformatics 25, 2078–2079 (2019).
doi: 10.1093/bioinformatics/btp352
Mizuguchi, G., Wu, W.-H., Alami, S. & Luk, E. in Methods in Enzymology (eds. Wu, C. & Allis, C. D.) vol. 512, 275–291 (Academic Press, 2012).

Auteurs

Aakash Basu (A)

Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Department of Physics, University of Illinois at Urbana-Champaign, Urbana, IL, USA.

Dmitriy G Bobrovnikov (DG)

Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.

Zan Qureshi (Z)

Department of Biophysics, Johns Hopkins University, Baltimore, MD, USA.

Tunc Kayikcioglu (T)

Department of Physics, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, IL, USA.

Thuy T M Ngo (TTM)

Department of Physics, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, IL, USA.

Anand Ranjan (A)

Department of Biology, Johns Hopkins University, Baltimore, MD, USA.

Sebastian Eustermann (S)

Department of Biochemistry, Ludwig-Maximilians-Universität, Munich, Germany.
Gene Center, Ludwig-Maximilians-Universität, Munich, Germany.

Basilio Cieza (B)

Department of Biophysics, Johns Hopkins University, Baltimore, MD, USA.

Michael T Morgan (MT)

Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.

Miroslav Hejna (M)

Department of Physics, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
Carl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL, USA.

H Tomas Rube (HT)

Department of Physics, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
Carl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL, USA.

Karl-Peter Hopfner (KP)

Department of Biochemistry, Ludwig-Maximilians-Universität, Munich, Germany.
Gene Center, Ludwig-Maximilians-Universität, Munich, Germany.

Cynthia Wolberger (C)

Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.

Jun S Song (JS)

Department of Physics, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
Carl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
Cancer Center at Illinois, University of Illinois, Urbana, IL, USA.

Taekjip Ha (T)

Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA. tjha@jhu.edu.
Department of Physics, University of Illinois at Urbana-Champaign, Urbana, IL, USA. tjha@jhu.edu.
Department of Biophysics, Johns Hopkins University, Baltimore, MD, USA. tjha@jhu.edu.
Department of Biomedical Engineering, Johns Hopkins University, Baltimore, MD, USA. tjha@jhu.edu.
Howard Hughes Medical Institute, Baltimore, MD, USA. tjha@jhu.edu.

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