Self-Assembly of a Designed Nucleoprotein Architecture through Multimodal Interactions

Subramanian, Rohit H.; Smith, Sarah J.; Alberstein, Robert G.; Bailey, Jake B.; Zhang, Ling; Cardone, Giovanni; Suominen, Lauri; Chami, Mohamed; Stahlberg, Henning; Baker, Timothy S.; Tezcan, F. Akif

doi:10.1021/acscentsci.8b00745

Title: Self-Assembly of a Designed Nucleoprotein Architecture through Multimodal Interactions

Abstract

The co-self-assembly of proteins and nucleic acids (NAs) produces complex biomolecular machines (e.g., ribosomes and telomerases) that represent some of the most daunting targets for biomolecular design. Despite significant advances in protein and DNA or RNA nanotechnology, the construction of artificial nucleoprotein complexes has largely been limited to cases that rely on the NA-mediated spatial organization of protein units, rather than a cooperative interplay between protein- and NA-mediated interactions that typify natural nucleoprotein assemblies. We report here a structurally well-defined synthetic nucleoprotein assembly that forms through the synergy of three types of intermolecular interactions: Watson–Crick base pairing, NA–protein interactions, and protein–metal coordination. The fine thermodynamic balance between these interactions enables the formation of a crystalline architecture under highly specific conditions.

Authors:

^[1];

^[1]; Alberstein, Robert G. ^[1]; Bailey, Jake B. ^[1]; Zhang, Ling ^[1]; Cardone, Giovanni ^[1]; Suominen, Lauri ^[1]; Chami, Mohamed ^[2]; Stahlberg, Henning ^[2]; Baker, Timothy S. ^[3];

^[4]

Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093, United States
C−CINA, Biozentrum, University of Basel, Mattenstrasse 26, 4058 Basel, Switzerland
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093, United States, Division of Biological Sciences, University of California, San Diego, La Jolla, California 92093, United States
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093, United States, Materials Science and Engineering, University of California, San Diego, La Jolla, California 92093, United States

Publication Date:: 2018-11-02

Research Org.:: Univ. of California, San Diego, CA (United States)

Sponsoring Org.:: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Science Foundation (NSF); National Inst. of Health (NIH) (United States)

OSTI Identifier:: 1482287

Alternate Identifier(s):: OSTI ID: 1508780

Grant/Contract Number:: SC0003844; AC02-76SF00515; DMR-1602537; T32GM112584-01; R01-GM033050

Resource Type:: Published Article

Journal Name:: ACS Central Science

Additional Journal Information:: Journal Name: ACS Central Science Journal Volume: 4 Journal Issue: 11; Journal ID: ISSN 2374-7943

Publisher:: American Chemical Society

Country of Publication:: United States

Language:: English

Subject:: 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY

Citation Formats


                    Subramanian, Rohit H., Smith, Sarah J., Alberstein, Robert G., Bailey, Jake B., Zhang, Ling, Cardone, Giovanni, Suominen, Lauri, Chami, Mohamed, Stahlberg, Henning, Baker, Timothy S., and Tezcan, F. Akif. Self-Assembly of a Designed Nucleoprotein Architecture through Multimodal Interactions.  United States: N. p., 2018. 
        Web.  doi:10.1021/acscentsci.8b00745.

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                    Subramanian, Rohit H., Smith, Sarah J., Alberstein, Robert G., Bailey, Jake B., Zhang, Ling, Cardone, Giovanni, Suominen, Lauri, Chami, Mohamed, Stahlberg, Henning, Baker, Timothy S., & Tezcan, F. Akif. Self-Assembly of a Designed Nucleoprotein Architecture through Multimodal Interactions.  United States.  doi:https://doi.org/10.1021/acscentsci.8b00745

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                    Subramanian, Rohit H., Smith, Sarah J., Alberstein, Robert G., Bailey, Jake B., Zhang, Ling, Cardone, Giovanni, Suominen, Lauri, Chami, Mohamed, Stahlberg, Henning, Baker, Timothy S., and Tezcan, F. Akif. Fri .  
        "Self-Assembly of a Designed Nucleoprotein Architecture through Multimodal Interactions".  United States.  doi:https://doi.org/10.1021/acscentsci.8b00745.

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@article{osti_1482287,

  title        = {Self-Assembly of a Designed Nucleoprotein Architecture through Multimodal Interactions},

  author       = {Subramanian, Rohit H. and Smith, Sarah J. and Alberstein, Robert G. and Bailey, Jake B. and Zhang, Ling and Cardone, Giovanni and Suominen, Lauri and Chami, Mohamed and Stahlberg, Henning and Baker, Timothy S. and Tezcan, F. Akif},

  abstractNote = {The co-self-assembly of proteins and nucleic acids (NAs) produces complex biomolecular machines (e.g., ribosomes and telomerases) that represent some of the most daunting targets for biomolecular design. Despite significant advances in protein and DNA or RNA nanotechnology, the construction of artificial nucleoprotein complexes has largely been limited to cases that rely on the NA-mediated spatial organization of protein units, rather than a cooperative interplay between protein- and NA-mediated interactions that typify natural nucleoprotein assemblies. We report here a structurally well-defined synthetic nucleoprotein assembly that forms through the synergy of three types of intermolecular interactions: Watson–Crick base pairing, NA–protein interactions, and protein–metal coordination. The fine thermodynamic balance between these interactions enables the formation of a crystalline architecture under highly specific conditions.},

  doi          = {10.1021/acscentsci.8b00745},

  journal      = {ACS Central Science},

  number       = 11,

  volume       = 4,

  place        = {United States},

  year         = {2018},

  month        = {11}

}

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DOI: https://doi.org/10.1021/acscentsci.8b00745

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Cited by: 2 works

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Figures / Tables:

Figure 1: Design of RIDC3−10a/b. (a) Schematic of RIDC3−DNA hybrids. Metal-binding residues are shown as cyan sticks on the RIDC3 surface. (b) Potential self-assembly outcomes for the RIDC3−DNA hybrids.

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Works referencing / citing this record:

Stimulus-responsive self-assembly of protein-based fractals by computational design
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Abstract

Citation Formats

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Stimulus-responsive self-assembly of protein-based fractals by computational design journal, June 2019

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