Proteomics

Dataset Information

0

Interaction of N-myc with TFIIIC5 DBD ΔΔ characterised by HDX-MS


ABSTRACT: Here we characterise the interaction between N-myc with TFIIIC5 DBD ΔΔ by HDX-MS.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Antonio Calabrese  

LAB HEAD: Antonio Calabrese

PROVIDER: PXD054754 | Pride | 2026-03-09

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
220208.DnX Other
220208NMyc.DnX Other
fbsaca_HDX_240205_03.raw.zip Raw
fbsaca_HDX_240205_05.raw.zip Raw
fbsaca_HDX_240205_07.raw.zip Raw
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Publications

Mechanism of interaction between the transactivation domain of N-myc and the DNA-binding surface of TFIIIC5.

Leen Eoin E   Yeoh Sharon S   Sahak Eka E   Mitchell Ellie E   Wildsmith Gemma G   Batchelor Matthew M   Calabrese Antonio N AN   Büchel Gabriele G   Bayliss Richard R  

Nucleic acids research 20260201 5


N-myc is a transcription factor, a powerful driver of cellular growth and an important oncoprotein. N-myc interacts with many factors, including the RNA Polymerase III assembly factor, TFIIIC, a six-subunit complex that is essential for the transcription of small, structured RNA. TFIIIC and N-myc mutually restrict each other's chromatin association, and their complex contributes to quality control in mRNA transcription. We previously demonstrated that the intrinsically disordered transactivation  ...[more]

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