Rok1p is a putative RNA helicase required for rRNA processing

Autor: David Tollervey, Jean-Paul Gélugne, M. Caizergues-Ferrer, J. Venema, Cécile Bousquet-Antonelli
Přispěvatelé: Biochemistry and Molecular Biology, Molecular and Computational Toxicology
Jazyk: angličtina
Rok vydání: 1997
Předmět:
Zdroj: Molecular and Cellular Biology, 17(6), 3398-3407. American Society for Microbiology
Venema, J, Bousquet-Antonelli, C, Gelugne, J-P, Caizergues-Ferrer, M & Tollervey, D 1997, ' Rok1p is a putative RNA helicase required for rRNA processing. ', Molecular and Cellular Biology, vol. 17, no. 6, pp. 3398-3407 . https://doi.org/10.1128/MCB.17.6.3398
Venema, J, Gelugne, J P, CaizerguesFerrer, M, Tollervey, D & Bousquet-Antonelli, C 1997, ' Rok1p is a putative RNA helicase required for rRNA processing ', Molecular and Cellular Biology, vol. 17, no. 6, pp. 3398-3407 . < http://mcb.asm.org/content/17/6/3398.abstract >
ISSN: 0270-7306
DOI: 10.1128/mcb.17.6.3398
Popis: The synthesis of ribosomes involves many small nucleolar ribonucleoprotein particles (snoRNPs) as transacting factors. Yeast strains lacking the snoRNA, snR10, are viable but are impaired in growth and delayed in the early pre-rRNA cleavages at sites A0 ,A 1 , and A2, which lead to the synthesis of 18S rRNA. The same cleavages are inhibited by genetic depletion of the essential snoRNP protein Gar1p. Screens for mutations showing synthetic lethality with deletion of the SNR10 gene or with a temperature-sensitive gar1 allele both identified the ROK1 gene, encoding a putative, ATP-dependent RNA helicase of the DEAD-box family. The ROK1 gene is essential for viability, and depletion of Rok1p inhibits pre-rRNA processing at sites A0 ,A 1, and A2, thereby blocking 18S rRNA synthesis. Indirect immunofluorescence by using a ProtA-Rok1p construct shows the protein to be predominantly nucleolar. These results suggest that Rok1p is required for the function of the snoRNP complex carrying out the early pre-rRNA cleavage reactions. Ribosome biogenesis in eukaryotes takes place largely in a specialized nuclear compartment, the nucleolus (reviewed in reference 43). Here, approximately 80 ribosomal proteins associate with the four mature rRNA molecules to form the large and small ribosomal subunits. Three of the four rRNAs (18S, 5.8S, and 25‐28S rRNA) are produced from a single precursor (pre-rRNA), which, in addition to the mature rRNA se
Databáze: OpenAIRE