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In vivo kinetics of U4/U6·U5 tri-snRNP formation in Cajal bodies
I. Novotný, M. Blažíková, D. Staněk, P. Herman, J. Malinsky
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 1992 do Před 2 měsíci
PubMed Central
od 1992 do Před 2 měsíci
Europe PubMed Central
od 1992 do Před 2 měsíci
Open Access Digital Library
od 1989-11-01
Open Access Digital Library
od 1997-01-01
PubMed
21177826
DOI
10.1091/mbc.e10-07-0560
Knihovny.cz E-zdroje
- MeSH
- antigeny nádorové genetika metabolismus MeSH
- buněčné jádro genetika metabolismus MeSH
- Cajalova tělíska genetika metabolismus MeSH
- HeLa buňky MeSH
- jaderné proteiny metabolismus MeSH
- kinetika MeSH
- lidé MeSH
- malý jaderný ribonukleoprotein U4-U6 genetika metabolismus MeSH
- malý jaderný ribonukleoprotein U5 genetika metabolismus MeSH
- molekulární modely MeSH
- nádorové buněčné linie MeSH
- prekurzory RNA genetika metabolismus MeSH
- proteiny vázající RNA genetika metabolismus MeSH
- ribonukleoproteiny malé jaderné genetika metabolismus MeSH
- RNA-helikasy genetika metabolismus MeSH
- sestřih RNA genetika MeSH
- spliceozomy genetika metabolismus MeSH
- vazba proteinů genetika MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
The U4/U6·U5 tri-small nuclear ribonucleoprotein particle (tri-snRNP) is an essential pre-mRNA splicing factor, which is assembled in a stepwise manner before each round of splicing. It was previously shown that the tri-snRNP is formed in Cajal bodies (CBs), but little is known about the dynamics of this process. Here we created a mathematical model of tri-snRNP assembly in CBs and used it to fit kinetics of individual snRNPs monitored by fluorescence recovery after photobleaching. A global fitting of all kinetic data determined key reaction constants of tri-snRNP assembly. Our model predicts that the rates of di-snRNP and tri-snRNP assemblies are similar and that ∼230 tri-snRNPs are assembled in one CB per minute. Our analysis further indicates that tri-snRNP assembly is approximately 10-fold faster in CBs than in the surrounding nucleoplasm, which is fully consistent with the importance of CBs for snRNP formation in rapidly developing biological systems. Finally, the model predicted binding between SART3 and a CB component. We tested this prediction by Förster resonance energy transfer and revealed an interaction between SART3 and coilin in CBs.
Citace poskytuje Crossref.org
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