RNase P

• リボヌクレアーゼP

関

ribonuclease P

WordNet

1. the 16th letter of the Roman alphabet (同)p
2. a river in western Thailand; a major tributary of the Chao Phraya (同)Ping River

PrepTutorEJDIC

1. parking
2. phosphorusの化学記号
3. palladiumの化学記号

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/11/08 19:26:54」(JST)

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Crystal structure of a bacterial ribonuclease P holoenzyme in complex with tRNA (yellow), showing metal ions involved in catalysis (pink spheres), PDB: 3Q1R​

Bacterial RNase P class A
Predicted secondary structure and sequence conservation of RNaseP_bact_a
Identifiers
Symbol	RNaseP_bact_a
Rfam	RF00010
Other data
RNA type	Gene; ribozyme
Domain(s)	Bacteria
GO	0008033 0004526 0030680
SO	0000386

Bacterial RNase P class B
Predicted secondary structure and sequence conservation of RNaseP_bact_b
Identifiers
Symbol	RNaseP_bact_b
Rfam	RF00011
Other data
RNA type	Gene; ribozyme
Domain(s)	Bacteria
GO	0008033 0004526 0030680
SO	0000386

Archaeal RNase P
Predicted secondary structure and sequence conservation of Archaeal RNase P
Identifiers
Symbol	RNaseP_arch
Rfam	RF00373
Other data
RNA type	Gene; ribozyme
Domain(s)	Archaea
GO	0008033 0004526 0030680
SO	0000386

Archaeal RNase P class T
Predicted secondary structure and sequence conservation of the small form of Archaeal RNase P found in the Thermoproteaceae
Identifiers
Symbol	RNaseP-T
Rfam	RF02357
Other data
RNA type	Gene; ribozyme
Domain(s)	Archaea
GO	0008033 0004526 0030680
SO	0000386

Ribonuclease P (EC 3.1.26.5, RNase P) is a type of ribonuclease which cleaves RNA. RNase P is unique from other RNases in that it is a ribozyme – a ribonucleic acid that acts as a catalyst in the same way that a protein based enzyme would. Its function is to cleave off an extra, or precursor, sequence of RNA on tRNA molecules. Further, RNase P is one of two known multiple turnover ribozymes in nature (the other being the ribosome), the discovery of which earned Sidney Altman and Thomas Cech the Nobel Prize in Chemistry in 1989: in the 1970s, Altman discovered the existence of precursor tRNA with flanking sequences and was the first to characterize RNase P and its activity in processing of the 5' leader sequence of precursor tRNA. Recent findings also reveal that RNase P has a new function. It has been shown that human nuclear RNase P is required for the normal and efficient transcription of various small noncoding RNAs, such as tRNA, 5S rRNA, SRP RNA and U6 snRNA genes, which are transcribed by RNA polymerase III, one of three major nuclear RNA polymerases in human cells.

In bacteria

Bacterial RNase P has two components: an RNA chain, called M1 RNA, and a polypeptide chain, or protein, called C5 protein. In vivo, both components are necessary for the ribozyme to function properly, but in vitro, the M1 RNA can act alone as a catalyst. The primary role of the C5 protein is to enhance the substrate binding affinity and the catalytic rate of the M1 RNA enzyme probably by increasing the metal ion affinity in the active site. The crystal structure of a bacterial RNase P holoenzyme with tRNA has been recently resolved, showing how the large, coaxially stacked helical domains of the RNase P RNA engage in shape selective recognition of the pre-tRNA target. This crystal structure confirms earlier models of substrate recognition and catalysis, identifies the location of the active site, and shows how the protein component increases RNase P functionality.

Bacterial RNase P class A and B

Ribonuclease P (RNase P) is a ubiquitous endoribonuclease, found in archaea, bacteria and eukarya as well as chloroplasts and mitochondria. Its best characterised activity is the generation of mature 5'-ends of tRNAs by cleaving the 5'-leader elements of precursor-tRNAs. Cellular RNase Ps are ribonucleoproteins (RNP). RNA from bacterial RNase Ps retains its catalytic activity in the absence of the protein subunit, i.e. it is a ribozyme. Isolated eukaryotic and archaeal RNase P RNA has not been shown to retain its catalytic function, but is still essential for the catalytic activity of the holoenzyme. Although the archaeal and eukaryotic holoenzymes have a much greater protein content than the bacterial ones, the RNA cores from all the three lineages are homologous—helices corresponding to P1, P2, P3, P4, and P10/11 are common to all cellular RNase P RNAs. Yet, there is considerable sequence variation, particularly among the eukaryotic RNAs.

In archaea

In archaea, RNase P ribonucleoproteins consist of 4-5 protein subunits that are associated with RNA. As revealed by in vitro reconstitution experiments these protein subunits are individually dispensable for tRNA processing that is essentially mediated by the RNA component. The structures of protein subunits of archaeal RNase P have been resolved by x-ray crystallography and NMR, thus revealing new protein domains and folding fundamental for function.

Using comparative genomics and improved computational methods, a radically minimized form of the RNase P RNA, dubbed "Type T", has been found in all complete genomes in the crenarchaeal phylogenetic family Thermoproteaceae, including species in the genera Pyrobaculum, Caldivirga and Vulcanisaeta. All retain a conventional catalytic domain, but lack a recognizable specificity domain. 5′ tRNA processing activity of the RNA alone was experimentally confirmed. The Pyrobaculum and Caldivirga RNase P RNAs are the smallest naturally occurring form yet discovered to function as trans-acting ribozymes. Loss of the specificity domain in these RNAs suggests potential altered substrate specificity.

It has recently been argued that the archaebacteriium Nanoarchaeum equitans does not possess RNase P. Computational and experimental studies failed to find evidence for its existence. In this organism the tRNA promoter is close to the tRNA gene and it is thought that transcription starts at the first base of the tRNA thus removing the requirement for RNase P.

In eukaryotes

Further information: Nuclear RNase P

In eukaryotes, such as humans and yeast, most RNase P consists of an RNA chain that is structurally similar to that found in bacteria as well as nine to ten associated proteins (as opposed to the single bacterial RNase P protein, C5). Five of these protein subunits exhibit homology to archaeal counterparts. These protein subunits of RNase P are shared with RNase MRP, a catalytic ribonucleoprotein involved in processing of ribosomal RNA in the nucleolus. RNase P from eukaryotes was only recently demonstrated to be a ribozyme. Accordingly, the numerous protein subunits of eucaryal RNase P have a minor contribution to tRNA processing per se, while they seem to be essential for the function of RNase P and RNase MRP in other biological settings, such as gene transcription and the cell cycle. Despite the bacterial origins of mitochondria and chloroplasts, plastids from higher animals and plants do not appear to contain an RNA-based RNase P. It has been shown that human mitochondrial RNase P is a protein and does not contain RNA. Spinach chloroplast RNase P has also been shown to function without an RNA subunit.

References

Further reading

• Nobel Lecture of Sidney Altman, Nobel prize in Chemistry 1989
• Frank, DN; Pace NR (1998). "Ribonuclease P: unity and diversity in a tRNA processing ribozyme". Annu Rev Biochem. 67: 153–180. doi:10.1146/annurev.biochem.67.1.153. PMID 9759486. 
• Brown, JW (1999). "The Ribonuclease P Database". Nucleic Acids Res. 27 (1): 314–. doi:10.1093/nar/27.1.314. PMC 148169. PMID 9847214. 

External links

• RNase P Database at ncsu.edu
• Page for Nuclear RNase P at Rfam
• Page for Archaeal RNase P at Rfam
• Page for Bacterial RNase P class A at Rfam
• Page for Bacterial RNase P class B at Rfam
• RNase P at the US National Library of Medicine Medical Subject Headings (MeSH)
• EC 3.1.26.5

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English Journal

• RNase P Protein Subunit, Rpp29, Represses Histone H3.3 Nucleosome Deposition.

• Newhart A1, Powers SL1, Shastrula PK2, Sierra I1, Joo LM1, Hayden JE1, Cohen AR3, Janicki SM4.
• Molecular biology of the cell.Mol Biol Cell.2016 Feb 3. pii: mbc.E15-02-0099. [Epub ahead of print]
• In mammals, histone H3.3 is a critical regulator of transcription state change and heritability at both euchromatin and heterochromatin. The H3.3-specific chaperone, DAXX, together with the chromatin-remodeling factor, ATRX, regulates H3.3 deposition and transcriptional silencing at repetitive DNA,
• PMID 26842893

• Natural antisense RNA promotes 3' end processing and maturation of MALAT1 lncRNA.

• Zong X1, Nakagawa S2, Freier SM3, Fei J4, Ha T4, Prasanth SG1, Prasanth KV5.
• Nucleic acids research.Nucleic Acids Res.2016 Jan 29. pii: gkw047. [Epub ahead of print]
• The RNase P-mediated endonucleolytic cleavage plays a crucial role in the 3' end processing and cellular accumulation of MALAT1, a nuclear-retained long noncoding RNA that promotes malignancy. The regulation of this cleavage event is largely undetermined. Here we characterize a broadly expressed nat
• PMID 26826711

• Simultaneous characterization of cellular RNA structure and function with in-cell SHAPE-Seq.

• Watters KE1, Abbott TR1, Lucks JB2.
• Nucleic acids research.Nucleic Acids Res.2016 Jan 29;44(2):e12. doi: 10.1093/nar/gkv879. Epub 2015 Sep 8.
• Many non-coding RNAs form structures that interact with cellular machinery to control gene expression. A central goal of molecular and synthetic biology is to uncover design principles linking RNA structure to function to understand and engineer this relationship. Here we report a simple, high-throu
• PMID 26350218

Japanese Journal

• 細菌におけるRNaseを介した代謝制御 : 産業微生物コリネ型細菌を例に

• 前田 智也,和地 正明
• 化学と生物 : 日本農芸化学会会誌 : 生命・食・環境 53(2), 99-106, 2015-02
• NAID 40020348968

• Evolutionary Analysis of Genes for S-RNase-based Self-incompatibility Reveals S Locus Duplications in the Ancestral Rosaceae

• , ,
• The Horticulture Journal advpub(0), 2015
• … The Solanaceae, the Rosaceae, and the Plantaginaceae have the S-RNase-based gametophytic SI (GSI) system, which uses S-RNase and F-box proteins as the pistil S and pollen S determinants, respectively. … Here, we investigated the evolutionary paths of the S-RNase genes by tracking their duplication patterns. …
• NAID 130005064826

• DNA Markers and the Molecular Mechanism of Self-(in)compatibility in Japanese Pear (Pyrus pyrifolia Nakai)

• The Horticulture Journal advpub(0), 2015
• Japanese pear (Pyrus pyrifolia Nakai) is an important Rosaceous fruit tree in Japan. This species exhibits gametophytic self-incompatibility (GSI), which is controlled by a single S-locus with multipl …
• NAID 130005064823

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★リンクテーブル★

リンク元	「リボヌクレアーゼP」「ribonuclease P」
関連記事	「P」「p」「Pd」

「リボヌクレアーゼP」

　　[★]

英

ribonuclease P, RNaseP, RNase P

同

RNアーゼP

関

リボ核蛋白質

「ribonuclease P」

　　[★]

リボヌクレアーゼP

関

RNase P

「P」

　　[★]

• プロリン proline
• P波 P wave
• リン phosphorus

　 　 　

「p」

　　[★]

• ピコ

10の-12乗

関

pico

「Pd」

　　[★] パラジウム palladium