Naslov
AtBPM1 protein is involved in RNA-directed DNA methylation in plants

Autori
Bauer, Nataša ; Jagić, Mateja ; Škiljaica, Andreja ; Markulin, Lucija ; Leljak Levanić Dunja

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
4th CONGRESS OF CROATIAN GENETICISTS with international participation / Hrvoje, Šarčević ; Đurđica, Ugarković ; Dušica, Vujaklija ; Ivan, Krešimir Svetec ; Marina, Svetec Miklenić - Zagreb : Hrvatsko genetičko društvo, 2018, 31-31

ISBN
978-953-57128-1-7

Skup
4th Congress of Croatian Geneticists with international participation

Mjesto i datum
Krk, Hrvatska, 26.09.2018. - 29.09.2018

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
MATH-BTB, RNA-directed DNA methylation, Arabidopsis, DMS3, RDM1

Sažetak
DNA methylation is one of several epigenetic mechanisms used by cells to control gene expression. Plant DNA methylation occurs at CG, CHG and CHH (H is A, C or T) sequences. Nonsymmetrical CHH methylation cannot be sustained by the maintenance and require de novo methylation in each cell cycle through a process called RNA-directed DNA methylation (RdDM). In this prosess the DDR complex target the methylation machinery to specific regions in the genome but the mechanism of DDR complex possitioning is still not clear. AtBPM1 belongs to the small family of Arabidopsis MATH and BTB domain proteins that are known as substrate-specific adaptors in the cullin3 dependent ubiquitin proteasom e pathway. Tandem affinity purification and yeast two hybrid assay revealed interaction of BPM1 with DMS3 and RDM1, crucial components of RdDM. Fluorescently tagged BPM1 and its truncated version with deletion of MATH or BTB domain showed that both domains are essential for accumulation of the protein in nucleolus, whilst co-localization show significant overlap of BPM1 with aforementioned RdDM components. Yeast two hybrid assay using truncated BPM1 protein missing MATH or BTB domain revealed that the cullin3-binding BTB domain had higher affinity for RDM1 interaction while both, MATH and BTB domains proved to be equally important for DMS3 interaction. New insights into BPM1 protein and its interaction partners indicate an important, cullin independent function of MATH-BTB protein family in RdDM.

Izvorni jezik
Engleski

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