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Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

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Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...
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Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction
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Cryo-EM structure of the CBC-ALYREF complex.

Bradley P Clarke, Alexia E Angelos, Menghan Mei

    Biorxiv : the Preprint Server for Biology
    |October 24, 2023
    PubMed
    Summary

    The nuclear cap binding complex (CBC) recruits mRNA export factors like ALYREF to facilitate gene expression. This study reveals the structural basis of this interaction, clarifying mRNA processing and export mechanisms.

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    Area of Science:

    • Molecular Biology
    • Structural Biology
    • Biochemistry

    Background:

    • Eukaryotic RNAs undergo 5' end modification with a 7-methylguanosine (m7G) cap.
    • The nuclear cap binding complex (CBC) recognizes the m7G cap and is crucial for mRNA metabolism.
    • CBC mediates mRNA export by interacting with ALYREF, a component of the TRanscription and EXport (TREX) complex.

    Purpose of the Study:

    • To elucidate the molecular mechanism of CBC-mediated recruitment of mRNA export machinery.
    • To determine the structural basis of the interaction between CBC and ALYREF.

    Main Methods:

    • Cryo-electron microscopy (cryo-EM) to determine the structure of the CBC-ALYREF complex.

    Main Results:

    • The first structure of the CBC in complex with the mRNA export factor ALYREF was determined.
    • The cryo-EM structure revealed direct contacts between the RRM domain of ALYREF and both NCBP1 and NCBP2 subunits of the CBC.
    • Structural comparisons provided insights into coordinated events in mRNA transcription, splicing, and export.

    Conclusions:

    • The structure provides a molecular understanding of how CBC recruits ALYREF for mRNA export.
    • This finding contributes to understanding the intricate processes of mRNA metabolism and transport in eukaryotes.