RAC protein directs the complete removal of the 3' external transcribed spacer by the Pac1 nuclease.
Mol Cell
; 9(2): 433-7, 2002 Feb.
Article
em En
| MEDLINE
| ID: mdl-11864615
ABSTRACT
In Schizosaccharomyces pombe, interdependency in rRNA processing is mediated by a large protein complex (RAC) which contains independent binding sites for each of the transcribed spacers. The RAC complex exhibits no nuclease activity but dramatically alters the efficiency and specificity of the Pac1 nuclease, leading to the complete removal of the 3' ETS. Furthermore, the affinity of RAC protein for mutant 3' ETS correlates closely with in vivo effects on rRNA processing, and changes which disrupt RAC protein binding also inhibit Pac1 nuclease cleavage at the 3' end of the 25S rRNA sequence. The observations indicate that, in the presence of the RAC protein/3' ETS complex, cleavage by the RNase III-like homolog is not restricted to the known intermediate sites but also is directed at the 3' end of the 25S rRNA.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
DNA Fúngico
/
RNA Fúngico
/
RNA Ribossômico
/
Proteínas Fúngicas
/
Precursores de RNA
/
Proteínas rac de Ligação ao GTP
/
DNA Espaçador Ribossômico
/
Proteínas de Schizosaccharomyces pombe
/
Endorribonucleases
Idioma:
En
Revista:
Mol Cell
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2002
Tipo de documento:
Article
País de afiliação:
Canadá