Loc1p is required for efficient assembly and nuclear export of the 60S ribosomal subunit

Urbinati, Carl R.; Gonsalvez, Graydon B.; Aris, John P.; Long, Roy

doi:10.1007/s00438-006-0151-7

Cited by 23 publications

(51 citation statements)

References 49 publications

(79 reference statements)

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“…13,14 This has also been shown for the yeast RNA-binding Loc1p, which has roles in rRNA processing as well as in the assembly and nucleocytoplasmic export of the 60S subunits. [15][16][17] Consistent with these findings, Ash1 mRNA has a cis-acting binding site for Loc1p and Puf6p, and it does not properly localize to the daughter cell in Loc1 and Puf6 mutant yeast. 18 Hence, ribosome biogenesis and translation machinery affect mRNA localization.…”

Section: Pumilio Puf Domain Rna-binding Proteins In Arabidopsismentioning

confidence: 57%

“…18 Hence, ribosome biogenesis and translation machinery affect mRNA localization. 16,17,19 Pumilio proteins are required to maintain germ-line stem cell identity in Drosophila, Caenorhabditis elegans and humans. In Drosophila, Pumilio acts together with Nanos to repress the translation of maternal hunchback RNA in the posterior end of the Drosophila embryo, thereby allowing abdomen formation.…”

Section: Pumilio Puf Domain Rna-binding Proteins In Arabidopsismentioning

confidence: 99%

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Pumilio Puf domain RNA-binding proteins in Arabidopsis

Abbasi

Park

Choi

2011

Plant Signaling & Behavior

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Section: Pumilio Puf Domain Rna-binding Proteins In Arabidopsismentioning

confidence: 57%

Section: Pumilio Puf Domain Rna-binding Proteins In Arabidopsismentioning

confidence: 99%

Pumilio Puf domain RNA-binding proteins in Arabidopsis

Abbasi

Park

Choi

2011

Plant Signaling & Behavior

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“…Ribosomes are composed of two subunits, a small subunit and a large subunit, 40S and 60S, respectively, in eukaryotic cells. In Saccharomyces cerevisiae, the 40S and 60S subunits are assembled from a large primary 35 S rRNA transcribed by RNA polymerase I. Processing of this rRNA yields 5.8S, 18S, and 25S rRNAs.…”

mentioning

confidence: 99%

The Roles of Puf6 and Loc1 in 60S Biogenesis Are Interdependent, and Both Are Required for Efficient Accommodation of Rpl43

Yang

Ting

Liang

et al. 2016

Journal of Biological Chemistry

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Puf6 and Loc1 have two important functional roles in the cells, asymmetric mRNA distribution and ribosome biogenesis. Puf6 and Loc1 are localized predominantly in the nucleolus. They bind ASH1 mRNA, repress its translation, and facilitate the transport to the daughter cells. Asymmetric mRNA distribution is important for cell differentiation. Besides their roles in mRNA localization, Puf6 and Loc1 have been shown to be involved in 60S biogenesis. In puf6⌬ or loc1⌬ cells, pre-rRNA processing and 60S export are impaired and 60S subunits are underaccumulated. The functional studies of Puf6 and Loc1 have been focused on ASH1 mRNA pathway, but their roles in 60S biogenesis are still not clear. In this study, we found that Puf6 and Loc1 interact directly with each other and both proteins interact with the ribosomal protein Rpl43 (L43e). Notably, the roles of Puf6 and Loc1 in 60S biogenesis are interdependent, and both are required for efficient accommodation of Rpl43. Loc1 is further required to maintain the protein level of Rpl43. Additionally, the recruitment of Rpl43 is required for the release of Puf6 and Loc1. We propose that Puf6 and Loc1 facilitate Rpl43 loading and are sequentially released from 60S after incorporation of Rpl43 into ribosomes in yeast.Almost every process in a cell is mediated by proteins, the products of translating mRNA by ribosomes. Ribosomes are composed of two subunits, a small subunit and a large subunit, 40S and 60S, respectively, in eukaryotic cells. In Saccharomyces cerevisiae, the 40S and 60S subunits are assembled from a large primary 35 S rRNA transcribed by RNA polymerase I. Processing of this rRNA yields 5.8S, 18S, and 25S rRNAs. The 5S rRNA is transcribed by RNA polymerase III separately (see reviews in Refs. 1-4). In yeast, 5S, 5.8S, and 25S (28S in higher eukaryotes) rRNA assemble with 39 ribosomal proteins to make up the 60S subunit, whereas 18S rRNA and 33 ribosomal proteins constitute the 40S subunit (5-7).Ribosome biogenesis is necessary for cell growth and proliferation. The synthesis of ribosome is a complex pathway in which over 200 trans-acting factors are involved. Many of the RNA folding, protein assembly, and maturation events are hierarchical, requiring the correct completion of one event to progress to the next event. This is seen in the assembly of ribosomal proteins onto the RNA in bacterial ribosome assembly (8) as well as in cytoplasmic maturation of the large subunit in yeast (9, 10). In addition, trans-acting factors also perform quality control steps for the assembly of the protein synthesis machinery. Syo1 facilitates the synchronized import of the two 5S rRNA-binding proteins, Rpl5 and Rpl11, to ensure stoichiometric the incorporation of these two proteins into the pre-60S subunits and also works as an assembly platform for the 5S ribonucleoprotein (RNP) (11,12). Release of the anti-association factor Tif6 requires elongation factor-like Efl1 and tRNAlike Sdo1 to confirm the integrity of the P-site (13-15). Transacting factors on cytoplasmic pre-40S subuni...

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“…A fourth nuclear factor, termed localization of ASH1 mRNA protein 1 (Loc1p), has been implicated in the assembly of nuclear premessenger ribonucleoprotein particles (mRNPs). Like Puf6p, Loc1p is a nuclear protein (13) with an enrichment in the nucleolus (14, 15) and participates in the assembly of the large ribosomal subunit (16)(17)(18).The composition of the nuclear ASH1 mRNP was previously analyzed by coimmunoprecipitation experiments. By using She2p as bait, Puf6p, Loc1p, and ASH1 mRNA were copurified (11,19).…”

mentioning

confidence: 99%

mentioning

confidence: 99%

Role of Loc1p in assembly and reorganization of nuclear ASH1 messenger ribonucleoprotein particles in yeast

Niedner

Müller

Moorthy

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Directional transport of mRNA is a universal feature in eukaryotes, requiring the assembly of motor-dependent RNA-transport particles. The cytoplasmic transport of mRNAs is preceded by the nuclear assembly of pre-messenger ribonucleoprotein particles (mRNPs). In budding yeast, the asymmetric synthesis of HO 1 (ASH1) pre-mRNP originates already cotranscriptionally and passes through the nucleolus before its nuclear export. The nucleolar localization of ASH1 mRNA protein 1 (Loc1p) is required for efficient ASH1 mRNA localization. Immunoprecipitation experiments have revealed that Loc1p forms cocomplexes with other components of the ASH1 transport complex. However, it remains unclear how Loc1p is recruited into this mRNP and why Loc1p is important for ASH1 mRNA localization. Here we demonstrate that Loc1p undergoes a direct and specific interaction with the ASH1 mRNA-binding Swi5p-dependent HO expression protein 2 (She2p). This cocomplex shows higher affinity and specificity for RNA bearing localization elements than the individual proteins. It also stabilizes the otherwise transient binding of She2p to ASH1 mRNA, suggesting that cooperative mRNA binding of Loc1p with She2p is the required nuclear function of Loc1p for ASH1 mRNA localization. After nuclear export, myosin-bound She3p joins the ASH1 mRNP to form a highly specific cocomplex with She2p and ASH1 mRNA. Because Loc1p is found only in the nucleus, it must be removed from the complex directly before or after export. In vitro and in vivo experiments indicate that the synergistic interaction of She2p and She3p displaces Loc1p from the ASH1 complex, allowing free Loc1p to rapidly reenter the nucle(ol)us. Together these findings suggest an ordered process of nuclear assembly and reorganization for the maturation of localizing ASH1 mRNPs.M essenger RNA localization is a universal feature of eukaryotes (1-3). By complementing transcriptional control (4), it fulfills a variety of functions, including the establishment of cell polarity and specialization of subcellular regions. In recent years, the directional transport of asymmetric synthesis of HO 1 (ASH1) mRNA in budding yeast has emerged as a particularly well-suited model to study mechanistic principles of RNA localization. Here, comparably few proteins participate in the directional transport of ASH1 mRNA and about 30 other transcripts (5, 6).Chromatin-immunoprecipitaton experiments revealed that the dedicated RNA-binding Swi5p-dependent HO expression protein 2 (She2p) binds already cotranscriptionally to nascent ASH1 mRNA (7, 8). Two additional RNA-binding proteins, pumiliohomology domain family protein 6 (Puf6p) and heterogeneous nuclear RNP K-like protein 1 (Khd1p), are also present in the nucleus, bind to ASH1 mRNA, and act in the cytoplasm as translational repressors during ASH1 transport (9-12). A fourth nuclear factor, termed localization of ASH1 mRNA protein 1 (Loc1p), has been implicated in the assembly of nuclear premessenger ribonucleoprotein particles (mRNPs). Like Puf6p, Loc1p is a nuclear protei...

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Loc1p is required for efficient assembly and nuclear export of the 60S ribosomal subunit

Cited by 23 publications

References 49 publications

Pumilio Puf domain RNA-binding proteins in Arabidopsis

Pumilio Puf domain RNA-binding proteins in Arabidopsis

The Roles of Puf6 and Loc1 in 60S Biogenesis Are Interdependent, and Both Are Required for Efficient Accommodation of Rpl43

Role of Loc1p in assembly and reorganization of nuclear ASH1 messenger ribonucleoprotein particles in yeast

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