Rpf2p, an Evolutionarily Conserved Protein, Interacts with Ribosomal Protein L11 and Is Essential for the Processing of 27 SB Pre-rRNA to 25 S rRNA and the 60 S Ribosomal Subunit Assembly inSaccharomyces cerevisiae

Morita, Daisuke; Miyoshi, Keita; Matsui, Yasuji; Toh‐e, Akio; Shinkawa, Hidenori; Miyakawa, Tokichi; Mizuta, Keiko

doi:10.1074/jbc.m203399200

Cited by 46 publications

(53 citation statements)

References 38 publications

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“…A subcomplex in preribosomes that contains ribosome assembly factors Rpf2 and Rrs1,ribosomal proteins rpL5 and rpL11,and 5S rRNA Previous yeast two-hybrid experiments revealed pairwise interactions between Rpf2, Rrs1, and rpL11 Morita et al 2002). In mature yeast ribosomes, rpL11 is adjacent to 5S rRNA and rpL5 ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Assembly factors Rpf2 and Rrs1 recruit 5S rRNA and ribosomal proteins rpL5 and rpL11 into nascent ribosomes

Zhang

Harnpicharnchai²,

Jakovljevic³

et al. 2007

Genes Dev.

180

271

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More than 170 proteins are necessary for assembly of ribosomes in eukaryotes. However, cofactors that function with each of these proteins, substrates on which they act, and the precise functions of assembly factors-e.g., recruiting other molecules into preribosomes or triggering structural rearrangements of pre-rRNPs-remain mostly unknown. Here we investigated the recruitment of two ribosomal proteins and 5S ribosomal RNA (rRNA) into nascent ribosomes. We identified a ribonucleoprotein neighborhood in preribosomes that contains two yeast ribosome assembly factors, Rpf2 and Rrs1, two ribosomal proteins, rpL5 and rpL11, and 5S rRNA. Interactions between each of these four proteins have been confirmed by binding assays in vitro. These molecules assemble into 90S preribosomal particles containing 35S rRNA precursor (pre-rRNA). Rpf2 and Rrs1 are required for recruiting rpL5, rpL11, and 5S rRNA into preribosomes. In the absence of association of these molecules with pre-rRNPs, processing of 27SB pre-rRNA is blocked. Consequently, the abortive 66S pre-rRNPs are prematurely released from the nucleolus to the nucleoplasm, and cannot be exported to the cytoplasm. In eukaryotes, 79 ribosomal proteins associate with ribosomal RNA (rRNA) to produce 40S and 60S ribosomal subunits (Woolford and Warner 1991). Three of the four rRNAs in mature ribosomes are derived from the 35S-45S rRNA precursor (pre-rRNA) transcribed by RNA polymerase I, while the fourth rRNA, 5S rRNA, is transcribed from separate genes by RNA polymerase III. The 35S-45S primary transcript is packaged into a 90S ribonucleoprotein particle (RNP), together with a subset of assembly factors and ribosomal proteins. Subsequent steps trigger folding, modification, and processing of prerRNAs and association of additional assembly factors and ribosomal proteins in 43S and 66S assembly intermediates. These pre-rRNPs undergo further maturation in the nucleolus, nucleoplasm, and then cytoplasm to form functional 40S and 60S ribosomal subunits, respectively ( Fig. 1A; FromontRacine et al. 2003;Raué 2003;Granneman and Baserga 2004). Preribosomal particles in the assembly pathway are distinguished by the presence of successive prerRNA processing intermediates (Fig. 1A). However, it is not clear into which of the consecutive preribosomes 5S rRNA and each ribosomal protein are incorporated, which assembly factors are required to recruit these molecules, or how they do so. Furthermore, the mechanisms by which constituents of nascent ribosomes facilitate folding, processing, and modification of pre-rRNAs remain elusive.5S rRNA is essential for maturation of preribosomes and for the function of mature ribosomes (Van Ryk et al. 1992;Dechampesme et al. 1999;Kiparisov et al. 2005). Steitz and coworkers defined a pathway of assembly of 5S rRNA into ribosomes in HeLa cells. Newly synthesized 5S pre-rRNA binds transiently to the La protein (Rinke and Steitz 1982;Yoo and Wolin 1994). Following 3Ј-end maturation, 5S rRNA binds to ribosomal protein rpL5, then assembles into ribosomes (...

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Section: Resultsmentioning

confidence: 99%

Assembly factors Rpf2 and Rrs1 recruit 5S rRNA and ribosomal proteins rpL5 and rpL11 into nascent ribosomes

Zhang

Harnpicharnchai²,

Jakovljevic³

et al. 2007

Genes Dev.

180

271

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“…Interactions among components of a subcomplex, such as the Nop7-or PeBoW-subcomplex (Lapik et al, 2004;Miles et al, 2005), the Rpf2-subcomplex (Morita et al, 2002;Miyoshi et al, 2004;Nariai et al, 2005;Zhang et al, 2007), or the Arx1-subcomplex (Lebreton et al, 2006), have been inferred from indirect yeast two-hybrid experiments in vivo, GST pulldown assays in vitro, or by assays for genetic interactions.…”

Section: Discussionmentioning

confidence: 99%

Interactions among Ytm1, Erb1, and Nop7 Required for Assembly of the Nop7-Subcomplex in Yeast Preribosomes

Tang

Sahasranaman

Jakovljevic

et al. 2008

MBoC

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In Saccharomyces cerevisiae, more than 180 assembly factors associate with preribosomes to enable folding of pre-rRNA, recruitment of ribosomal proteins, and processing of pre-rRNAs to produce mature ribosomes. To examine the molecular architecture of preribosomes and to connect this structure to functions of each assembly factor, assembly subcomplexes have been purified from preribosomal particles. The Nop7-subcomplex contains three assembly factors: Nop7, Erb1, and Ytm1, each of which is necessary for conversion of 27SA 3 pre-rRNA to 27SB S pre-rRNA. However, interactions among these three proteins and mechanisms of their recruitment and function in pre-rRNPs are poorly understood. Here we show that Ytm1, Erb1, and Nop7 assemble into preribosomes in an interdependent manner. We identified which domains within Ytm1, Erb1, and Nop7 are necessary for their interaction with each other and are sufficient for recruitment of each protein into preribosomes. Dominant negative effects on growth and ribosome biogenesis caused by overexpressing truncated Ytm1, Erb1, or Nop7 constructs, and recessive phenotypes of the truncated proteins revealed not only interaction domains but also other domains potentially important for each protein to function in ribosome biogenesis. Our data suggest a model for the architecture of the Nop7-subcomplex and provide potential functions of domains of each protein.

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“…4) We found that Rrs1 is essential for growth, is localized in the nucleus with enrichment into the nucleolus, and is required for the maturation of 25S rRNA and the assembly of 60S ribosomal subunits. 4,5) We also found that Rrs1 interacts with ribosomal protein L11 and L5-5S rRNA complex, 6,7) and that the normal functioning of Rrs1 is required for the export of 60S ribosomal subunits from the nucleolus to the cytoplasm. 8) Rrs1 is highly conserved in eukaryotes, and is 36.8% identical to its human homolog.…”

mentioning

confidence: 93%

Genetic Interaction between Ribosome Biogenesis and Inositol Polyphosphate Metabolism inSaccharomyces cerevisiae

Horigome¹,

Ikeda²,

Okada³

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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Rpf2p, an Evolutionarily Conserved Protein, Interacts with Ribosomal Protein L11 and Is Essential for the Processing of 27 SB Pre-rRNA to 25 S rRNA and the 60 S Ribosomal Subunit Assembly inSaccharomyces cerevisiae

Cited by 46 publications

References 38 publications

Assembly factors Rpf2 and Rrs1 recruit 5S rRNA and ribosomal proteins rpL5 and rpL11 into nascent ribosomes

Assembly factors Rpf2 and Rrs1 recruit 5S rRNA and ribosomal proteins rpL5 and rpL11 into nascent ribosomes

Interactions among Ytm1, Erb1, and Nop7 Required for Assembly of the Nop7-Subcomplex in Yeast Preribosomes

Genetic Interaction between Ribosome Biogenesis and Inositol Polyphosphate Metabolism inSaccharomyces cerevisiae

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