mRNA recognition and packaging by the human transcription–export complex

Newly made mRNAs are processed and packaged into mature ribonucleoprotein complexes (mRNPs) and are recognized by the essential transcription–export complex (TREX) for nuclear export 1 , 2 . However, the mechanisms of mRNP recognition and three-dimensional mRNP organization are poorly understood 3 ....

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Vydáno v:Nature (London) Ročník 616; číslo 7958; s. 828 - 835
Hlavní autoři: Pacheco-Fiallos, Belén, Vorländer, Matthias K., Riabov-Bassat, Daria, Fin, Laura, O’Reilly, Francis J., Ayala, Farja I., Schellhaas, Ulla, Rappsilber, Juri, Plaschka, Clemens
Médium: Journal Article
Jazyk:angličtina
Vydáno: London Nature Publishing Group UK 27.04.2023
Nature Publishing Group
Témata:
101/28
101/58
631/337/1645
631/45/535
631/535/1258/1259
631/535/1258/1260
Active Transport, Cell Nucleus
Cell Nucleus - genetics
Cell Nucleus - metabolism
Cryoelectron Microscopy
Electron microscopy
Exons
Globules
Humanities and Social Sciences
Humans
Interfaces
Microscopy
multidisciplinary
Mutation
Nuclear transport
Packaging
Proteins
Recognition
RNA, Messenger - biosynthesis
RNA, Messenger - genetics
RNA, Messenger - metabolism
Science
Science (multidisciplinary)
Tomography
Transcription, Genetic
ISSN:0028-0836, 1476-4687, 1476-4687
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Popis
Shrnutí:Newly made mRNAs are processed and packaged into mature ribonucleoprotein complexes (mRNPs) and are recognized by the essential transcription–export complex (TREX) for nuclear export 1 , 2 . However, the mechanisms of mRNP recognition and three-dimensional mRNP organization are poorly understood 3 . Here we report cryo-electron microscopy and tomography structures of reconstituted and endogenous human mRNPs bound to the 2-MDa TREX complex. We show that mRNPs are recognized through multivalent interactions between the TREX subunit ALYREF and mRNP-bound exon junction complexes. Exon junction complexes can multimerize through ALYREF, which suggests a mechanism for mRNP organization. Endogenous mRNPs form compact globules that are coated by multiple TREX complexes. These results reveal how TREX may simultaneously recognize, compact and protect mRNAs to promote their packaging for nuclear export. The organization of mRNP globules provides a framework to understand how mRNP architecture facilitates mRNA biogenesis and export. Cryo-electron microscopy and tomography structures of reconstituted and endogenous human mRNA ribonucleoprotein complexes bound to the transcription–export complex reveal how mRNAs are packaged and recognized for nuclear export.
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ISSN:0028-0836
1476-4687
1476-4687
DOI:10.1038/s41586-023-05904-0