関: RIP

WordNet

an organelle in the cytoplasm of a living cell; they attach to mRNA and move down it one codon at a time and then stop until tRNA brings the required amino acid; when it reaches a stop codon it falls apart and releases the completed protein molecule for u
any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"

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リボゾーム(細胞質に含まれ,蛋白質とリボ核酸から成る微小粒子)
蛋白(たんばく)質

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/09/19 14:26:49」(JST)

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A ribosome-inactivating protein is a protein synthesis inhibitor that acts at the ribosome.^[2]

A number of bacterial and plant toxins act by inhibiting protein synthesis in eukaryotic cells. The toxins of the Shiga and ricin family inactivate 60S ribosomal subunits by an N-glycosidic cleavage, which releases a specific adenine base from the sugar-phosphate backbone of 28S rRNA.^[3]^[4]^[5] Members of the family include shiga and shiga-like toxins, and type I (e.g. trichosanthin and luffin) and type II (e.g. ricin, agglutinin and abrin) ribosome inactivating proteins (RIPs). All these toxins are structurally related. RIPs have been of considerable interest because of their potential use, conjugated with monoclonal antibodies, as immunotoxins to treat cancers. Further, trichosanthin has been shown to have potent activity against HIV-1-infected T cells and macrophages.^[6] Elucidation of the structure-function relationships of RIPs has therefore become a major research effort. It is now known that RIPs are structurally related. A conserved glutamic residue has been implicated in the catalytic mechanism;^[7] this lies near a conserved arginine, which also plays a role in catalysis.^[8]

Examples include:

Abrin
Trichosanthin
Ricin
Saporin

They exist in bacteria and plants.^[9]

It should also be noted that only a minority of RIPs are toxic to humans when consumed, and proteins of this family are found in the vast majority of plants used for human consumption, such as Rice, Maize and Barley.

References

^ Monzingo AF, Collins EJ, Ernst SR, Irvin JD, Robertus JD (October 1993). "The 2.5 A structure of pokeweed antiviral protein". J. Mol. Biol. 233 (4): 705–15. doi:10.1006/jmbi.1993.1547. PMID 8411176.
^ Ribosome Inactivating Proteins at the US National Library of Medicine Medical Subject Headings (MeSH)
^ Igarashi K, Endo Y, Tsurugi K, Takeda Y, Ogasawara T, Yutsudo T (1988). "Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosomes. RNA N-glycosidase activity of the toxins". Eur. J. Biochem. 171 (1): 45–50. doi:10.1111/j.1432-1033.1988.tb13756.x. PMID 3276522.
^ May MJ, Hartley MR, Roberts LM, Krieg PA, Osborn RW, Lord JM (1989). "Ribosome inactivation by ricin A chain: a sensitive method to assess the activity of wild-type and mutant polypeptides". EMBO J. 8 (1): 301–308. PMC 400803. PMID 2714255.
^ Funatsu G, Islam MR, Minami Y, Sung-Sil K, Kimura M (1991). "Conserved amino acid residues in ribosome-inactivating proteins from plants". Biochimie. 73 (7): 1157–1161. doi:10.1016/0300-9084(91)90160-3. PMID 1742358.
^ Zhou K, Fu Z, Chen M, Lin Y, Pan K (1994). "Structure of trichosanthin at 1.88 A resolution". Proteins. 19 (1): 4–13. doi:10.1002/prot.340190103. PMID 8066085.
^ Collier RJ, Calderwood SB, Mekalanos JJ, Hovde CJ (1988). "Evidence that glutamic acid 167 is an active-site residue of Shiga-like toxin I". Proc. Natl. Acad. Sci. U.S.A. 85 (8): 2568–2572. doi:10.1073/pnas.85.8.2568. PMC 280038. PMID 3357883.
^ Monzingo AF, Collins EJ, Ernst SR, Irvin JD, Robertus JD (1993). "The 2.5 A structure of pokeweed antiviral protein". J. Mol. Biol. 233 (4): 705–715. doi:10.1006/jmbi.1993.1547. PMID 8411176.
^ Mak AN, Wong YT, An YJ, et al. (2007). "Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site". Nucleic Acids Res. 35 (18): 6259–67. doi:10.1093/nar/gkm687. PMC 2094058. PMID 17855394.

This article incorporates text from the public domain Pfam and InterPro IPR001574

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1. プロテインＳ欠乏症 protein s deficiency
2. プロテインＣ欠乏症 protein c deficiency
3. 維持透析患者における蛋白質摂取 protein intake in maintenance hemodialysis patients
4. 甲状腺刺激ホルモンおよび甲状腺刺激ホルモン放出ホルモンに対する抵抗性 resistance to thyrotropin and thyrotropin releasing hormone
5. Molecular genetics of the thalassemic syndromes

English Journal

Plant Translation Initiation Complex eIFiso4F Directs Pokeweed Antiviral Protein to Selectively Depurinate Uncapped Tobacco Etch Virus RNA.

Domashevskiy AV1, Williams S1, Kluge C1, Cheng SY1.
Biochemistry.Biochemistry.2017 Nov 1. doi: 10.1021/acs.biochem.7b00598. [Epub ahead of print]
PMID 29064680

Which Plant Proteins Are Involved in Antiviral Defense? Review on In Vivo and In Vitro Activities of Selected Plant Proteins against Viruses.

Musidlak O1, Nawrot R2, Goździcka-Józefiak A3.
International journal of molecular sciences.Int J Mol Sci.2017 Nov 1;18(11). pii: E2300. doi: 10.3390/ijms18112300.
PMID 29104238

Targeted dianthin is a powerful toxin to treat pancreatic carcinoma when applied in combination with the glycosylated triterpene SO1861.

Bhargava C1, Dürkop H2, Zhao X1, Weng A1,3, Melzig MF3, Fuchs H1.
Molecular oncology.Mol Oncol.2017 Nov;11(11):1527-1543. doi: 10.1002/1878-0261.12115. Epub 2017 Sep 15.
PMID 28755527

Japanese Journal

Purification and characterization of abelesculin, a novel ribosome-inactivating protein from the mature seeds of Abelmoschus esculentus

Kondo Toshiya,Yoshikawa Takafumi
Journal of natural medicines 61(2), 170-174, 2007-05-20
NAID 10018832759

Cochinin B, a Novel Ribosome-Inactivating Protein from the Seeds of Momordica cochinchinensis(Biochemistry)

Chuethong Juthamas,Oda Kohei,Sakurai Hiroaki [他],SAIKI Ikuo,LEELAMANIT Wichet
Biological & pharmaceutical bulletin 30(3), 428-432, 2007-03-01
… Cochinin B, a novel ribosome-inactivating protein (RIP) with a molecular weight of 28kDa, was purified from the seeds of Momordica cochinchinensis (Cucurbitaceae). … The isolation procedure entailed ammonium sulfate precipitation, cation-exchange chromatography on SP Sepharose column and size-exclusion chromatography on Superdex 75 column with a fast protein liquid chromatography (FPLC) system. …
NAID 110006239179

2P009 Fluorescence spectroscopic studies on the structure-dynamics-function correlation of ribosome-inactivating proteins(29. Protein structure and dynamics (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

Fukunaga Yukihiro,Nishimoto Etsuko,Otosu Takuhiro,Yamashita Katsumi,Yamashita Shoji
生物物理 46(SUPPLEMENT_2), S298, 2006-10-01
NAID 110006193970

「RIP」

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Ribosome-inactivating protein
	Structure of pokeweed antiviral protein.
Identifiers
Symbol	RIP
Pfam	PF00161
InterPro	IPR001574
PROSITE	PDOC00248
SCOP	1paf
SUPERFAMILY	1paf
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

　　[★]

受容体共役タンパク質、制限的膜内切断、((略))(植物)ボソーム不活性化タンパク質

関: receptor-interacting protein、regulated intramembrane proteolysis、ribosome inactivating protein

「リボソーム不活性化タンパク質」

　　[★]

英: ribosome inactivating protein、RIP
関: 受容体共役タンパク質、制限的膜内切断

「type 1 ribosome inactivating protein」

　　[★]

1型リボソーム不活性化タンパク質

「type 2 ribosome inactivating protein」

　　[★]

2型リボソーム不活性化タンパク質

[pmid8411176-1] Monzingo AF, Collins EJ, Ernst SR, Irvin JD, Robertus JD (October 1993). "The 2.5 A structure of pokeweed antiviral protein". J. Mol. Biol. 233 (4): 705–15. doi:10.1006/jmbi.1993.1547. PMID 8411176.

[2] Ribosome Inactivating Proteins at the US National Library of Medicine Medical Subject Headings (MeSH)

[PUB00001357-3] Igarashi K, Endo Y, Tsurugi K, Takeda Y, Ogasawara T, Yutsudo T (1988). "Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosomes. RNA N-glycosidase activity of the toxins". Eur. J. Biochem. 171 (1): 45–50. doi:10.1111/j.1432-1033.1988.tb13756.x. PMID 3276522.

[PUB00001175-4] May MJ, Hartley MR, Roberts LM, Krieg PA, Osborn RW, Lord JM (1989). "Ribosome inactivation by ricin A chain: a sensitive method to assess the activity of wild-type and mutant polypeptides". EMBO J. 8 (1): 301–308. PMC 400803. PMID 2714255.

[PUB00000690-5] Funatsu G, Islam MR, Minami Y, Sung-Sil K, Kimura M (1991). "Conserved amino acid residues in ribosome-inactivating proteins from plants". Biochimie. 73 (7): 1157–1161. doi:10.1016/0300-9084(91)90160-3. PMID 1742358.

[PUB00004990-6] Zhou K, Fu Z, Chen M, Lin Y, Pan K (1994). "Structure of trichosanthin at 1.88 A resolution". Proteins. 19 (1): 4–13. doi:10.1002/prot.340190103. PMID 8066085.

[PUB00004654-7] Collier RJ, Calderwood SB, Mekalanos JJ, Hovde CJ (1988). "Evidence that glutamic acid 167 is an active-site residue of Shiga-like toxin I". Proc. Natl. Acad. Sci. U.S.A. 85 (8): 2568–2572. doi:10.1073/pnas.85.8.2568. PMC 280038. PMID 3357883.

[PUB00003312-8] Monzingo AF, Collins EJ, Ernst SR, Irvin JD, Robertus JD (1993). "The 2.5 A structure of pokeweed antiviral protein". J. Mol. Biol. 233 (4): 705–715. doi:10.1006/jmbi.1993.1547. PMID 8411176.

[pmid17855394-9] Mak AN, Wong YT, An YJ, et al. (2007). "Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site". Nucleic Acids Res. 35 (18): 6259–67. doi:10.1093/nar/gkm687. PMC 2094058. PMID 17855394.

リンク元	「RIP」「リボソーム不活性化タンパク質」
拡張検索	「type 1 ribosome inactivating protein」「type 2 ribosome inactivating protein」

匿名

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案内

案内

ribosome inactivating protein