Comment on "Ancient origins of allosteric activation in a Ser-Thr kinase"

Park, Y.; Patton, J. E. J.; Hochberg, G. K. A.; Thornton, J. W.

doi:10.1126/science.abc8301

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Comment on "Ancient origins of allosteric activation in a Ser-Thr kinase"

Park, Y., Patton, J. E. J., Hochberg, G. K. A., & Thornton, J. W. (2020). Comment on "Ancient origins of allosteric activation in a Ser-Thr kinase". Science, 370(6519). doi:10.1126/science.abc8301.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000A-76A5-7 Version Permalink: https://hdl.handle.net/21.11116/0000-000A-76A6-6

Genre: Journal Article

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https://www.ncbi.nlm.nih.gov/pubmed/33214251 (Any fulltext) Open Access status unknown

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Park, Y., Author
Patton, J. E. J., Author
Hochberg, G. K. A.¹, Author
Thornton, J. W., Author

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1Max Planck Research Group Evolutionary Biochemistry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266300

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Free keywords: Allosteric Regulation Amino Acid Sequence *Aurora Kinases/metabolism Phylogeny

Abstract: Hadzipasic et al (Reports, 21 February 2020, p. 912) used ancestral sequence reconstruction to identify historical sequence substitutions that putatively caused Aurora kinases to evolve allosteric regulation. We show that their results arise from using an implausible phylogeny and sparse sequence sampling. Addressing either problem reverses their inferences: Allostery and the amino acids that confer it were not gained during the diversification of eukaryotes but were lost in a subgroup of Fungi.

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Dates: Date issued: 2020-11-21

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Identifiers: Other: 33214251
DOI: 10.1126/science.abc8301
ISSN: 1095-9203 (Electronic)0036-8075 (Linking)

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Title: Science

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Pages: - Volume / Issue: 370 (6519) Sequence Number: - Start / End Page: - Identifier: -