Structure of KAP1 tripartite motif identifies molecular interfaces required for retroelement silencing.
Transcription of transposable parts is tightly regulated to stop genome injury. KRAB domain-containing zinc finger proteins (KRAB-ZFPs) and KRAB-associated protein 1 (KAP1/TRIM28) play a key position in regulating retrotransposons. KRAB-ZFPs acknowledge particular retrotransposon sequences and recruit KAP1, inducing the meeting of an epigenetic silencing advanced, with chromatin transforming actions that repress transcription of the focused retrotransposon and adjoining genes.
Our biophysical and structural knowledge present that the tripartite motif (TRIM) of KAP1 kinds antiparallel dimers, which additional assemble into tetramers and higher-order oligomers in a concentration-dependent method. Structure-based mutations within the B-box 1 area forestall higher-order oligomerization with out important loss of retrotransposon silencing exercise, indicating that, in distinction to different TRIM-family proteins, self-assembly just isn’t important for KAP1 operate.
The crystal construction of the KAP1 TRIM dimer identifies the KRAB area binding website within the coiled-coil area close to the dyad. Mutations at this website abolished KRAB binding and transcriptional silencing exercise of KAP1.
This work identifies the interplay interfaces within the KAP1 TRIM accountable for self-association and KRAB binding and establishes their position in retrotransposon silencing.
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