A novel small nucleolar RNA (U16) is encoded inside a ribosomal protein intron and originates by processing of the pre-mRNA.

The gene encoding ribosomal protein L1 in Xenopus laevis is known to be posttranscriptionally regulated; the third intron can be processed from the pre-mRNA in two alternative ways, resulting either in the production of L1 mRNA or in the release of a small nucleolar RNA (U16). The formation of splicing complexes was studied in vivo by oocyte microinjection. We show that spliceosome assembly is impaired on the L1 third intron and that the low efficiency of the process is due to the presence of suboptimal consensus sequences. An analysis of heterogeneous nuclear ribonucleoprotein (hnRNP) distribution was also performed, revealing a distinct site for hnRNP C binding proximal to the 5' end of the L1 third intron. Cleavage, leading to the production of the small nucleolar RNA U16, occurs in the same position, and we show that conditions under which hnRNP C binding is reduced result in an increase of the processing activity of the intron.

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U21, a novel small nucleolar RNA with a 13 nt. complementarity to 28S rRNA, is encoded in an intron of ribosomal protein L5 gene in chicken and mammals

Nucleic Acids Research ◽

10.1093/nar/22.20.4073 ◽

1994 ◽

Vol 22 (20) ◽

pp. 4073-4081 ◽

Cited By ~ 28

Author(s):

Liang-Hu Qu ◽

Monique Nicoloso ◽

Bernard Michot ◽

Marie-Claude Azum ◽

Michèle Caizergues-Ferrer ◽

...

Keyword(s):

Ribosomal Protein ◽

28S Rrna ◽

Small Nucleolar Rna ◽

Ribosomal Protein L5 ◽

Nucleolar Rna

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A small nucleolar RNA is processed from an intron of the human gene encoding ribosomal protein S3.

Genes & Development ◽

10.1101/gad.7.7a.1176 ◽

1993 ◽

Vol 7 (7a) ◽

pp. 1176-1190 ◽

Cited By ~ 95

Author(s):

K T Tycowski ◽

M D Shu ◽

J A Steitz

Keyword(s):

Ribosomal Protein ◽

Human Gene ◽

Small Nucleolar Rna ◽

Gene Encoding ◽

Ribosomal Protein S3 ◽

Nucleolar Rna

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RNA-protein interactions in the nuclei of Xenopus oocytes: complex formation and processing activity on the regulatory intron of ribosomal protein gene L1.

Molecular and Cellular Biology ◽

10.1128/mcb.14.10.6975 ◽

1994 ◽

Vol 14 (10) ◽

pp. 6975-6982 ◽

Cited By ~ 8

Author(s):

B Santoro ◽

E De Gregorio ◽

E Caffarelli ◽

I Bozzoni

Keyword(s):

Ribosomal Protein ◽

Protein Interactions ◽

Ribosomal Protein Gene ◽

Small Nucleolar Rna ◽

Gene Encoding ◽

Hnrnp C ◽

Processing Activity ◽

Low Efficiency ◽

Nucleolar Rna

The gene encoding ribosomal protein L1 in Xenopus laevis is known to be posttranscriptionally regulated; the third intron can be processed from the pre-mRNA in two alternative ways, resulting either in the production of L1 mRNA or in the release of a small nucleolar RNA (U16). The formation of splicing complexes was studied in vivo by oocyte microinjection. We show that spliceosome assembly is impaired on the L1 third intron and that the low efficiency of the process is due to the presence of suboptimal consensus sequences. An analysis of heterogeneous nuclear ribonucleoprotein (hnRNP) distribution was also performed, revealing a distinct site for hnRNP C binding proximal to the 5' end of the L1 third intron. Cleavage, leading to the production of the small nucleolar RNA U16, occurs in the same position, and we show that conditions under which hnRNP C binding is reduced result in an increase of the processing activity of the intron.

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