Pregled bibliografske jedinice broj: 723941
MATH-BTB domain protein AtBPM1 directly interact with DMS3, important component of RNA-directed DNA methylation in plants
MATH-BTB domain protein AtBPM1 directly interact with DMS3, important component of RNA-directed DNA methylation in plants // FEBS-EMBO 2014
Pariz, Francuska, 2014. str. 306-306 (poster, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 723941 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
MATH-BTB domain protein AtBPM1 directly interact with DMS3, important component of RNA-directed DNA methylation in plants
Autori
Bauer, Nataša ; Leljak-Levanić, Dunja ; Vuković, Rosemary ; Razdorov, Genadij
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Skup
FEBS-EMBO 2014
Mjesto i datum
Pariz, Francuska, 30.08.2014. - 04.09.2014
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
chromatin remodeling; protein-protein interactions; RNA-directed DNA methylation.
Sažetak
In Arabidopsis thaliana, the MATH-BTB (BPM) proteins comprise a small family of six members. BPMs act as substrate-binding adaptors for the Cullin3-based ubiquitin E3 ligase, and interect with a broad range of Ethylene response factor/apetala2 transcription factors and with homeodomain-leucine zipper transcription factor ATHB6 affecting fatty acid metabolism and abscisic acid signaling. We showed previously that AtBPM1, localizes predominantly in nucleolus of plant cells indicating a Cullin3 independent function. To further elucidate the molecular function of AtBPM1, we identified AtBPM1 binding and functional partners using tandem affinity purification and mass spectrometry. Different stress-related proteins were identified in AtBPM1 protein complexes such as Catalases CAT2 and CAT3, Nucleoside diphosphate kinase III, Glycine-rich RNA-binding proteins GRP7 and GRP8, MLP-like protein 423, Polyketide cyclase/dehydrase and lipid transport superfamily protein. Moreover, we have identified a set of DNA repair and chromatin remodeling proteins, such as Nucleosome assembly protein NAP1, Tudor-SN proteins, DNA-damage- repair/toleration protein DRT102, WD-40 repeat family protein/beige-related, Chromatin remodeling 34, DNA mismatch repair protein Msh6-1 as well as a known components of RNA-directed DNA methylation, defective in meristem silencing 3 DMS3 and RNA-directed DNA methylation 1 RDM1. Furthermore, direct interaction of AtBPM1 and DMS3 was confirmed by yeast two hybrid and pull down assays and DNA methylation in plants overexpressing AtBPM1 was reduced. These results, for the first time, links MATH-BTB proteins with DNA methylation and related mechanisms.
Izvorni jezik
Engleski
Znanstvena područja
Biologija
POVEZANOST RADA
Ustanove:
Farmaceutsko-biokemijski fakultet, Zagreb,
Prirodoslovno-matematički fakultet, Zagreb