The nuclear protein p30 specifically interacts with a nuclear matrix attachment region from the rat genome

• Autorzy: Fedorov A , Lukyanov D. , Rogolinski J. , Widlak P. , Podgornaya O. , Rzeszowska-Wolny J.
• Języki publikacji: EN

Abstrakty

EN

In our previous study, a 454 bp DNA fragment was isolated from rat genomic DNA as an element which interacts with nuclear matrix proteins, i.e. a Matrix Associated Region (MAR). Computer analyses revealed that the right half of this fragment, named RME (Rat MAR Element), possesses a high matrix association potential and is likely to be responsible for the matrix association of the whole sequence. RME was used as a probe in an electrophoretic mobility shift assay (EMSA), and with the use of Southwestern blotting, a rat liver nuclear protein which binds specifically to it was identified. Its molecular mass was estimated by SDS-PAGE as 30 kDa (p30). Polyclonal antibodies raised against protein-RME complexes caused a super-shift of specific complexes in EMSA, and bound to p30 in nuclear extracts of rat liver in Western blotting. The immunofluorescence labelling of a rat embryonic fibroblast cell monolayer with anti-p30 antibody revealed a mainly intranuclear pattern of staining.

Słowa kluczowe

EN

matrix associated region; chromatin organization; protein-DNA interaction; electrophoretic mobility shift assay; genome; rat

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 2004
• Tom: 09
• Numer: 1
• Opis fizyczny: p.153-165,fig.,ref.

Twórcy

autor

Fedorov A

• Russian Academy of Science, Tikhoretsky pr.4, 194064 St.Petersburg, Russia

autor

Lukyanov D.

autor

Rogolinski J.

autor

Widlak P.

autor

Podgornaya O.

autor

Rzeszowska-Wolny J.

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