Characterization of <i>RPR1</i> an Essential Gene Encoding the RNA Component of <i>Saccharomyces cerevisiae</i> Nuclear RNase P

Lee, J Y; Rohlman, Christopher E.; Molony, Lisa A.; Engelke, David R.

doi:10.1128/mcb.11.2.721-730.1991

Cited by 9 publications

(1 citation statement)

References 61 publications

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“…For most tRNAs, removal of the 3' trailer sequence occurs after removal of the 5' leader by RNase P (Fig. 1) (Lee et al 1991;O'Connor and Peebles 1991). As in E. coli (Li and Deutscher 1996), removal of the 3' trailer sequence in eukaryotes is catalyzed by a combination of endonucleases and exonucleases.…”

Section: ' Trailer Removal Catalyzed By Different Exonucleases and En...mentioning

confidence: 99%

The life and times of a tRNA

Phizicky

Hopper

2023

RNA

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The study of eukaryotic tRNA processing has given rise to an explosion of new information and insights in the last several years. We now have unprecedented knowledge of each step in the tRNA processing pathway, revealing unexpected twists in biochemical pathways, multiple new connections with regulatory pathways, and numerous biological effects of defects in processing steps that have profound consequences throughout eukaryotes, leading to growth phenotypes in the yeast Saccharomyces cerevisiae and to neurological and other disorders in humans. This review highlights seminal new results within the pathways that comprise the life of a tRNA, from its birth after transcription until its death by decay. We focus on new findings and revelations in each step of the pathway including the end-processing and splicing steps, many of the numerous modifications throughout the main body and anticodon loop of tRNA that are so crucial for tRNA function, the intricate tRNA trafficking pathways, and the quality control decay pathways, as well as the biogenesis and biology of tRNA-derived fragments. We also describe the many interactions of these pathways with signaling and other pathways in the cell.

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Section: ' Trailer Removal Catalyzed By Different Exonucleases and En...mentioning

confidence: 99%

The life and times of a tRNA

Phizicky

Hopper

2023

RNA

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Interactions among the protein and RNA subunits ofSaccharomyces cerevisiaenuclear RNase P

Houser-Scott

Xiao

Millikin

et al. 2002

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

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Ribonuclease P (RNase P) is a ubiquitous endoribonuclease that cleaves precursor tRNAs to generate mature 5 termini. Although RNase P from all kingdoms of life have been found to have essential RNA subunits, the number and size of the protein subunits ranges from one small protein in bacteria to at least nine proteins of up to 100 kDa. In Saccharomyces cerevisiae nuclear RNase P, the enzyme is composed of ten subunits: a single RNA and nine essential proteins. The spatial organization of these components within the enzyme is not yet understood. In this study we examine the likely binary protein-protein and protein-RNA subunit interactions by using directed two-and three-hybrid tests in yeast. Only two protein subunits, Pop1p and Pop4p, specifically bind the RNA subunit. Pop4p also interacted with seven of the other eight protein subunits. The remaining protein subunits all showed one or more specific proteinprotein interactions with the other integral protein subunits. Of particular interest was the behavior of Rpr2p, the only protein subunit found in RNase P but not in the closely related enzyme, RNase MRP. Rpr2p interacts strongly with itself as well as with Pop4p. Similar interactions with self and Pop4p were also detected for Snm1p, the only unique protein subunit so far identified in RNase MRP. This observation is consistent with Snm1p and Rpr2p serving analogous functions in the two enzymes. This study provides a low-resolution map of the multisubunit architecture of the ribonucleoprotein enzyme, nuclear RNase P from S. cerevisiae. Ribonuclease P (RNase P) is an essential endoribonuclease that acts early in tRNA biogenesis to remove the 5Ј leader sequences of precursor tRNAs (pretRNAs) (1-3). The enzyme has been identified in every organism tested, in all kingdoms of life. In most cases, the enzyme is composed of a single RNA subunit and one or more protein subunits (1, 4). The RNA subunit forms the catalytic core of the enzyme, and the bacterial and some archaeal RNA subunits alone are catalytic in vitro (5-7). In contrast, no eukaryotic RNase P RNA subunits have been shown to be catalytic in the absence of protein. In bacteria, RNase P is composed of a catalytic RNA subunit and a single small protein subunit. Studies on the bacterial RNase P protein suggest that the protein plays a role in substrate recognition (8)(9)(10)(11). Recent data show that at least one form of archaeal RNase P consists of four or more proteins and a single RNA subunit (12). Moreover, the identified archaeal proteins appear to be homologs of the eukaryotic RNase P proteins and not the bacterial proteins (T. A. Hall and J. W. Brown, personal communication).Eukaryotic nuclear RNase P contains an RNA subunit similar in size to its bacterial and archaeal counterparts, containing all of the most conserved ''critical regions'' from the bacterial consensus structure (13). However, the protein content is far more complex and is absolutely required for activity. Human nuclear RNase P appears to contain at least ten proteins (14-19). At le...

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Retrograde nuclear import of tRNA precursors is required for modified base biogenesis in yeast

Ohira

Suzuki

2011

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

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The retrograde movement of tRNAs from the cytoplasm to the nucleus occurs constitutively in eukaryotic cells but its functional significance remains unclear. We show evidence suggesting that in Saccharomyces cerevisiae, a spliced tRNA precursor must be imported into the nucleus before the biogenesis of a modified base can occur. Wybutosine (yW) is a modified base adjacent to the anticodon of tRNA Phe and is required for accurate decoding. Glucose starvation or overexpression of the nuclear tRNA binding protein Trz1p both caused nuclear retention of cytoplasmic tRNAs, impaired the yW synthesis, and induced the accumulation of its intermediate , N 1 -methylgunanosine (m 1 G), showing that the postspliced tRNA Phe is imported to the nucleus, where m 1 G is formed by Trm5p, after which it is reexported to the cytoplasm, where the yW synthesis is completed by cytoplasmic enzymes.posttranscriptional modification | tRNA processing | subcellular localization | RNA mass spectrometry T o generate sufficient amounts of the mature tRNAs that are required for protein synthesis, it is important that the tRNA precursors are processed and modified appropriately. In eukaryotes, primary tRNAs are transcribed by RNA polymerase III and then subjected to consecutive processing events, including trimming of the 5′ leader and 3′ trailer sequences, the addition of the CCA sequence to the 3′ terminus, the decoration with var-

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Characterization of RPR1 an Essential Gene Encoding the RNA Component of Saccharomyces cerevisiae Nuclear RNase P

Cited by 9 publications

References 61 publications

The life and times of a tRNA

The life and times of a tRNA

Interactions among the protein and RNA subunits ofSaccharomyces cerevisiaenuclear RNase P

Retrograde nuclear import of tRNA precursors is required for modified base biogenesis in yeast

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