Genetic interaction mapping informs integrative structure determination of protein complexes-Reference-Cited by-同舟云学术

Genetic interaction mapping informs integrative structure determination of protein complexes

Published:2020-12-11 Issue:6522 Volume:370 Page:
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Braberg Hannes¹²^ORCID,Echeverria Ignacia¹²³^ORCID,Bohn Stefan¹²⁴^ORCID,Cimermancic Peter³^ORCID,Shiver Anthony⁵^ORCID,Alexander Richard¹^ORCID,Xu Jiewei¹²⁴^ORCID,Shales Michael¹²,Dronamraju Raghuvar⁶,Jiang Shuangying⁷,Dwivedi Gajendradhar⁸,Bogdanoff Derek⁹,Chaung Kaitlin K.⁹^ORCID,Hüttenhain Ruth¹²⁴^ORCID,Wang Shuyi¹,Mavor David²³,Pellarin Riccardo³^ORCID,Schneidman Dina³^ORCID,Bader Joel S.¹⁰^ORCID,Fraser James S.²³^ORCID,Morris John¹¹^ORCID,Haber James E.⁸,Strahl Brian D.⁶,Gross Carol A.¹²,Dai Junbiao⁷^ORCID,Boeke Jef D.¹³¹⁴¹⁵¹⁶^ORCID,Sali Andrej²³¹¹^ORCID,Krogan Nevan J.¹²⁴¹⁷^ORCID

Affiliation:

1. Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158, USA.

2. Quantitative Biosciences Institute, University of California, San Francisco, San Francisco, CA 94158, USA.

3. Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, San Francisco, CA 94158, USA.

4. Gladstone Institutes, San Francisco, CA 94158, USA.

5. Graduate Group in Biophysics, University of California San Francisco, San Francisco, CA 94158, USA.

6. Department of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.

7. CAS Key Laboratory of Quantitative Engineering Biology, Guangdong Provincial Key Laboratory of Synthetic Genomics and Shenzhen Key Laboratory of Synthetic Genomics, Shenzhen Institute of Synthetic Biology, Shenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China.

8. Department of Biology and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454, USA.

9. Center for Advanced Technology, Department of Biophysics and Biochemistry, University of California, San Francisco, San Francisco, CA 94158, USA.

10. Department of Biomedical Engineering, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

11. Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94158, USA.

12. Department of Microbiology and Immunology and Department of Cell and Tissue Biology, University of California, San Francisco, San Francisco, CA 94158, USA.

13. NYU Langone Health, New York, NY 10016, USA.

14. High Throughput Biology Center and Department of Molecular Biology & Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

15. Institute for Systems Genetics and Department of Biochemistry and Molecular Pharmacology, NYU Langone Health, New York, NY 10016, USA.

16. Department of Biomedical Engineering, NYU Tandon School of Engineering, Brooklyn, NY 11201, USA.

17. Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.

Abstract

From phenotype to structure Much insight has come from structures of macromolecular complexes determined by methods such as crystallography or cryo–electron microscopy. However, looking at transient complexes remains challenging, as does determining structures in the context of the cellular environment. Braberg et al. used an integrative approach in which they mapped the phenotypic profiles of a comprehensive set of mutants in a protein complex in the context of gene deletions or environmental perturbations (see the Perspective by Wang). By associating the similarity between phenotypic profiles with the distance between residues, they determined structures for the yeast histone H3-H4 complex, subunits Rpb1-Rpb2 of yeast RNA polymerase II, and subunits RpoB-RpoC of bacterial RNA polymerase. Comparison with known structures shows that the accuracy is comparable to structures determined based on chemical cross-links. Science , this issue p. eaaz4910 ; see also p. 1269

Funder

National Institutes of Health

National Natural Science Foundation of China

National Key Research and Development Program of China Stem Cell and Translational Research

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference144 articles.

1. Integrating Diverse Data for Structure Determination of Macromolecular Assemblies

2. Structural Probing of a Protein Phosphatase 2A Network by Chemical Cross-Linking and Mass Spectrometry

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