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  Genetic interaction mapping informs integrative structure determination of protein complexes

Braberg, H., Echeverria, I., Bohn, S., Cimermancic, P., Shiver, A., Alexander, R., et al. (2020). Genetic interaction mapping informs integrative structure determination of protein complexes. Science, 370(6522): eaaz4910. doi:10.1126/science.aaz4910.

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 Creators:
Braberg, Hannes1, Author
Echeverria, Ignacia1, Author
Bohn, Stefan2, Author              
Cimermancic, Peter1, Author
Shiver, Anthony1, Author
Alexander, Richard1, Author
Xu, Jiewei1, Author
Shales, Michael1, Author
Dronamraju, Raghuvar1, Author
Jiang, Shuangying1, Author
Dwivedi, Gajendradhar1, Author
Bogdanoff, Derek1, Author
Chaung, Kaitlin K.1, Author
Huttenhain, Ruth1, Author
Wang, Shuyi1, Author
Mavor, David1, Author
Pellarin, Riccardo1, Author
Schneidman, Dina1, Author
Bader, Joel S.1, Author
Fraser, James S.1, Author
Morris, John1, AuthorHaber, James E.1, AuthorStrahl, Brian D.1, AuthorGross, Carol A.1, AuthorDai, Junbiao1, AuthorBoeke, Jef D.1, AuthorSali, Andrej1, AuthorKrogan, Nevan J.1, Author more..
Affiliations:
1external, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: LINKING MASS-SPECTROMETRY; RNA-POLYMERASE; CROSS-LINKING; HISTONE H3; MOLECULAR ARCHITECTURE; HIGH-RESOLUTION; H3K56 ACETYLATION; SET2 METHYLATION; INTERACTION MAP; CELL-CYCLEScience & Technology - Other Topics;
 Abstract: Determining structures of protein complexes is crucial for understanding cellular functions. Here, we describe an integrative structure determination approach that relies on in vivo measurements of genetic interactions. We construct phenotypic profiles for point mutations crossed against gene deletions or exposed to environmental perturbations, followed by converting similarities between two profiles into an upper bound on the distance between the mutated residues. We determine the structure of the yeast histone H3-H4 complex based on similar to 500,000 genetic interactions of 350 mutants. We then apply the method to subunits Rpb1-Rpb2 of yeast RNA polymerase II and subunits RpoB-RpoC of bacterial RNA polymerase. The accuracy is comparable to that based on chemical cross-links; using restraints from both genetic interactions and cross-links further improves model accuracy and precision. The approach provides an efficient means to augment integrative structure determination with in vivo observations.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published online
 Pages: 68
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000597271300037
DOI: 10.1126/science.aaz4910
 Degree: -

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Title: Science
  Abbreviation : Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 370 (6522) Sequence Number: eaaz4910 Start / End Page: - Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1