Sökning: id:"swepub:oai:prod.swepub.kib.ki.se:1955417" >
A novel conserved R...
A novel conserved RNA-binding domain protein, RBD-1, is essential for ribosome biogenesis
-
Bjork, P (författare)
-
Bauren, G (författare)
-
Jin, SB (författare)
-
visa fler...
-
Tong, YG (författare)
-
- Burglin, TR (författare)
- Karolinska Institutet
-
Hellman, U (författare)
-
Wieslander, L (författare)
-
visa färre...
-
(creator_code:org_t)
- American Society for Cell Biology (ASCB), 2002
- 2002
- Engelska.
-
Ingår i: Molecular biology of the cell. - : American Society for Cell Biology (ASCB). - 1059-1524 .- 1939-4586. ; 13:10, s. 3683-3695
- Relaterad länk:
-
https://europepmc.or...
-
visa fler...
-
http://kipublication...
-
https://doi.org/10.1...
-
visa färre...
Abstract
Ämnesord
Stäng
- Synthesis of the ribosomal subunits from pre-rRNA requires a large number of trans-acting proteins and small nucleolar ribonucleoprotein particles to execute base modifications, RNA cleavages, and structural rearrangements. We have characterized a novel protein, RNA-binding domain-1 (RBD-1), that is involved in ribosome biogenesis. This protein contains six consensus RNA-binding domains and is conserved as to sequence, domain organization, and cellular location from yeast to human. RBD-1 is essential in Caenorhabditis elegans. In the dipteran Chironomus tentans, RBD-1 (Ct-RBD-1) binds pre-rRNA in vitro and anti-Ct-RBD-1 antibodies repress pre-rRNA processing in vivo. Ct-RBD-1 is mainly located in the nucleolus in an RNA polymerase I transcription-dependent manner, but it is also present in discrete foci in the interchromatin and in the cytoplasm. In cytoplasmic extracts, 20–30% of Ct-RBD-1 is associated with ribosomes and, preferentially, with the 40S ribosomal subunit. Our data suggest that RBD-1 plays a role in structurally coordinating pre-rRNA during ribosome biogenesis and that this function is conserved in all eukaryotes.
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas