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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:
ORCiD logo [1]; ORCiD logo [1];  [1];  [1];  [1];  [1];  [1];  [2];  [2];  [3]; ORCiD logo [4]
  1. Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093, United States
  2. C−CINA, Biozentrum, University of Basel, Mattenstrasse 26, 4058 Basel, Switzerland
  3. 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
  4. 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:
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.
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
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.
@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}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
DOI: https://doi.org/10.1021/acscentsci.8b00745

Citation Metrics:
Cited by: 2 works
Citation information provided by
Web of Science

Figures / Tables:

Figure 1 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
journal, June 2019


    Figures/Tables have been extracted from DOE-funded journal article accepted manuscripts.