Key result
Proximity labeling reveals nascent small nuclear RNAs drive Cajal body formation by assembling RNA-binding proteins.
Why the study?
Although techniques exist to identify components of cellular bodies, a comprehensive method for analyzing both static and dynamic states has not been established.
An antibody-based in situ biotinylation technique reveals that nascent snRNAs transcribed in Cajal bodies assemble RNA-binding proteins to drive CB formation.
Preclinical mechanism only; leaves open translation to human nuclear organization.
Membrane-less subcellular compartments play important roles in various cellular functions. Although techniques exist to identify components of cellular bodies, a comprehensive method for analyzing both static and dynamic states has not been established. Here, we apply an antibody-based in situ biotinylation proximity-labeling technique to identify components of static and dynamic nuclear bodies. Using this approach, we comprehensively identify DNA, RNA, and protein components of Cajal bodies (CBs) and then clarify their interactome. By inhibiting transcription, we capture dynamic changes in CBs. Our analysis reveals that nascent small nuclear RNAs (snRNAs) transcribed in CBs contribute to CB formation by assembling RNA-binding proteins, including frontotemporal dementia-related proteins, RNA-binding motif proteins, and heterogeneous nuclear ribonucleoproteins.
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Noguchi et al. (2024) studied Cajal body formation. Antibody-based in situ biotinylation proximity-labeling technique was evaluated on Identification of DNA, RNA, and protein components of Cajal bodies and their interactome. An antibody-based in situ biotinylation proximity-labeling technique revealed that nascent small nuclear RNAs transcribed in Cajal bodies contribute to their formation by assembling RNA-binding proteins.
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