On the evolution of chaperones and cochaperones and the expansion of proteomes across the Tree of Life.
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| Title: | On the evolution of chaperones and cochaperones and the expansion of proteomes across the Tree of Life. |
|---|---|
| Authors: | Rebeaud, Mathieu E.1, Mallik, Saurav2, Goloubinoff, Pierre1 pierre.goloubinoff@unil.ch, Tawfik, Dan S.2 |
| Source: | Proceedings of the National Academy of Sciences of the United States of America. 5/25/2021, Vol. 118 Issue 21, p1-10. 10p. |
| Subjects: | Heat shock proteins, Adenosine triphosphate, Messenger RNA, Exchange |
| Abstract: | Across the Tree of Life (ToL), the complexity of proteomes varies widely. Our systematic analysis depicts that from the simplest archaea to mammals, the total number of proteins per proteome expanded ~200-fold. Individual proteins also became larger, and multidomain proteins expanded ~50-fold. Apart from duplication and divergence of existing proteins, completely new proteins were born. Along the ToL, the number of different folds expanded ~5-fold and fold combinations ~20-fold. Proteins prone to misfolding and aggregation, such as repeat and beta-rich proteins, proliferated ~600-fold and, accordingly, proteins predicted as aggregationprone became 6-fold more frequent in mammalian compared with bacterial proteomes. To control the quality of these expanding proteomes, core chaperones, ranging from heat shock proteins 20 (HSP20s) that prevent aggregation to HSP60, HSP70, HSP90, and HSP100 acting as adenosine triphosphate (ATP)-fueled unfolding and refolding machines, also evolved. However, these core chaperones were already available in prokaryotes, and they comprise ~0.3% of all genes from archaea to mammals. This challenge--roughly the same number of core chaperones supporting a massive expansion of proteomes--was met by 1) elevation of messenger RNA (mRNA) and protein abundances of the ancient generalist core chaperones in the cell, and 2) continuous emergence of new substrate-binding and nucleotide-exchange factor cochaperones that function cooperatively with core chaperones as a network. [ABSTRACT FROM AUTHOR] |
| Copyright of Proceedings of the National Academy of Sciences of the United States of America is the property of National Academy of Sciences and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 150551725 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: On the evolution of chaperones and cochaperones and the expansion of proteomes across the Tree of Life. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Rebeaud%2C+Mathieu+E%2E%22">Rebeaud, Mathieu E.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Mallik%2C+Saurav%22">Mallik, Saurav</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Goloubinoff%2C+Pierre%22">Goloubinoff, Pierre</searchLink><relatesTo>1</relatesTo><i> pierre.goloubinoff@unil.ch</i><br /><searchLink fieldCode="AR" term="%22Tawfik%2C+Dan+S%2E%22">Tawfik, Dan S.</searchLink><relatesTo>2</relatesTo> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Proceedings+of+the+National+Academy+of+Sciences+of+the+United+States+of+America%22">Proceedings of the National Academy of Sciences of the United States of America</searchLink>. 5/25/2021, Vol. 118 Issue 21, p1-10. 10p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Heat+shock+proteins%22">Heat shock proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Adenosine+triphosphate%22">Adenosine triphosphate</searchLink><br /><searchLink fieldCode="DE" term="%22Messenger+RNA%22">Messenger RNA</searchLink><br /><searchLink fieldCode="DE" term="%22Exchange%22">Exchange</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Across the Tree of Life (ToL), the complexity of proteomes varies widely. Our systematic analysis depicts that from the simplest archaea to mammals, the total number of proteins per proteome expanded ~200-fold. Individual proteins also became larger, and multidomain proteins expanded ~50-fold. Apart from duplication and divergence of existing proteins, completely new proteins were born. Along the ToL, the number of different folds expanded ~5-fold and fold combinations ~20-fold. Proteins prone to misfolding and aggregation, such as repeat and beta-rich proteins, proliferated ~600-fold and, accordingly, proteins predicted as aggregationprone became 6-fold more frequent in mammalian compared with bacterial proteomes. To control the quality of these expanding proteomes, core chaperones, ranging from heat shock proteins 20 (HSP20s) that prevent aggregation to HSP60, HSP70, HSP90, and HSP100 acting as adenosine triphosphate (ATP)-fueled unfolding and refolding machines, also evolved. However, these core chaperones were already available in prokaryotes, and they comprise ~0.3% of all genes from archaea to mammals. This challenge--roughly the same number of core chaperones supporting a massive expansion of proteomes--was met by 1) elevation of messenger RNA (mRNA) and protein abundances of the ancient generalist core chaperones in the cell, and 2) continuous emergence of new substrate-binding and nucleotide-exchange factor cochaperones that function cooperatively with core chaperones as a network. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Proceedings of the National Academy of Sciences of the United States of America is the property of National Academy of Sciences and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1073/pnas.2020885118 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 10 StartPage: 1 Subjects: – SubjectFull: Heat shock proteins Type: general – SubjectFull: Adenosine triphosphate Type: general – SubjectFull: Messenger RNA Type: general – SubjectFull: Exchange Type: general Titles: – TitleFull: On the evolution of chaperones and cochaperones and the expansion of proteomes across the Tree of Life. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Rebeaud, Mathieu E. – PersonEntity: Name: NameFull: Mallik, Saurav – PersonEntity: Name: NameFull: Goloubinoff, Pierre – PersonEntity: Name: NameFull: Tawfik, Dan S. IsPartOfRelationships: – BibEntity: Dates: – D: 25 M: 05 Text: 5/25/2021 Type: published Y: 2021 Identifiers: – Type: issn-print Value: 00278424 Numbering: – Type: volume Value: 118 – Type: issue Value: 21 Titles: – TitleFull: Proceedings of the National Academy of Sciences of the United States of America Type: main |
| ResultId | 1 |
