Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
Field | Value |
---|---|
Namespace | Cellular component |
Short description | Ribonuclease MRP complex |
Full defintion | A ribonucleoprotein complex that contains an RNA molecule of the snoRNA family, and cleaves the rRNA precursor as part of rRNA transcript processing. It also has other roles: In S. cerevisiae it is involved in cell cycle-regulated degradation of daughter cell-specific mRNAs, while in mammalian cells it also enters the mitochondria and processes RNAs to create RNA primers for DNA replication. |
Subterm of |
The relationship of GO:0000172 with other GO terms.
Relationship type | GO terms |
---|---|
Is a | |
Regulates | n.a. |
Part of | n.a. |
Positively regulates | n.a. |
Negatively regulates | n.a. |
A force layout showing the ancestor tree for GO:0000172, and its immediate children. If you wish to explore the tree dynamically, please use the GO Explorer.
This table contains additional metadata associated with the GO entry's definition field.
Field | Value |
---|---|
GOC | sgd_curators |
PMID | Subcellular partitioning of MRP RNA assessed by ultrastructural and biochemical analysis. J Cell Biol. 1994 Mar; 124 (6): 871–82.PMID: 7510714 A small RNA encoded within the nucleus is an essential subunit of a RNA processing endonuclease (RNase MRP) hypothesized to generate primers for mitochondrial DNA replication from the heavy strand origin of replication. Controversy has arisen, however, concerning the authenticity of an intramitochondrial pool of MRP RNA, and has called into question the existence of pathways for nucleo-mitochondrial transport of nucleic acids in animal cells. In an effort to resolve this controversy, we combined ultrastructural in situ hybridization and biochemical techniques to assess the subcellular partitioning of MRP RNA. Cryosections of mouse cardiomyocytes were hybridized with biotin-labeled RNA probes complementary to different regions of MRP RNA and varying in length from 115 to 230 nucleotides, followed by immunogold labeling. In addition, we transfected mouse C2C12 myogenic cells with constructs bearing mutated forms of the mouse MRP RNA gene and compared the relative abundance of the resulting transcripts to that of control RNAs within whole cell and mitochondrial fractions. In the former analysis we observed preferential localization of MRP RNA to nucleoli and mitochondria in comparison to the nucleoplasm and cytoplasm. In the latter series of studies we observed that wild-type MRP RNA partitions to the mitochondrial fraction by comparison to other RNA transcripts that are localized to the extramitochondrial cytoplasmic space (28S rRNA) or to the nucleoplasm (U1 snRNA). Deletions within 5' or 3' regions of the MRP RNA gene produced transcripts that remain competent for mitochondrial targeting. In contrast, deletion of the midportion of the coding region (nt 118 to 175) of the MRP RNA gene resulted in transcripts that fail to partition to the mitochondrial fraction. We conclude that an authentic intramitochondrial pool of MRP RNA is present in these actively respiring cells, and that specific structural determinants within the MRP RNA molecule permit it to be partitioned to mitochondria. |
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
Transcript | Name | Description | GO terms | GO count |
---|---|---|---|---|
– | Ribonucleases P/MRP protein subunit POP1; TAIR: AT2G47300.2 ribonuclease Ps; Swiss-Prot: sp|Q99575|POP1_HUMAN Ribonucleases P/MRP protein subunit POP1; TrEMBL-Plants: tr|I1MI98|I1MI98_SOYBN Uncharacterized protein; Found in the gene: LotjaGi3g1v0302000 | 3 | ||
– | Ribonucleases P/MRP protein subunit POP1; TAIR: AT2G47300.2 ribonuclease Ps; Swiss-Prot: sp|Q99575|POP1_HUMAN Ribonucleases P/MRP protein subunit POP1; TrEMBL-Plants: tr|V7AJR0|V7AJR0_PHAVU Uncharacterized protein; Found in the gene: LotjaGi4g1v0245400 | 3 | ||
– | Ribonucleases P/MRP protein subunit POP1; TAIR: AT2G47300.2 ribonuclease Ps; Swiss-Prot: sp|Q99575|POP1_HUMAN Ribonucleases P/MRP protein subunit POP1; TrEMBL-Plants: tr|V7AJR0|V7AJR0_PHAVU Uncharacterized protein; Found in the gene: LotjaGi4g1v0245400 | 3 |
A list of co-occurring GO terms within the L. japonicus gene space:
GO term | Namespace | Name | Observations | Saturation (%) |
---|---|---|---|---|
Cellular component | Nucleolar ribonuclease P complex | 1 | 33.33 |