Human mitochondrial tRNA quality control in health and disease: A channelling mechanism?
Mutations in human mitochondrial tRNA genes are associated with a number of multisystemic disorders. These single nucleotide substitutions in various domains of tRNA molecules may affect different steps of tRNA biogenesis. Often, the prominent decrease of aminoacylation and/or steady-state levels of...
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| Veröffentlicht in: | RNA biology 2012-01, Vol.9 (1), p.33-39 |
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| creator | Belostotsky, Ruth Frishberg, Yaacov Entelis, Nina |
| description | Mutations in human mitochondrial tRNA genes are associated with a number of multisystemic disorders. These single nucleotide substitutions in various domains of tRNA molecules may affect different steps of tRNA biogenesis. Often, the prominent decrease of aminoacylation and/or steady-state levels of affected mitochondrial tRNA have been demonstrated in patients' tissues and in cultured cells.
Similar effect has been observed for pathogenic mutations in nuclear genes encoding mitochondrial aminoacyl-tRNA-synthetases, while over-expression of mitochondrial aminoacyl-tRNA synthetases or elongation factor EF-Tu rescued mutated tRNAs from degradation.
In this review we summarize experimental data concerning the possible regulatory mechanisms governing mitochondrial tRNA steady-state levels, and propose a hypothesis based on the tRNA channelling principle. According to this hypothesis, interaction of mitochondrial tRNA with proteins ensures not only tRNA synthesis, maturation and function, but also protection from degradation. Mutations perturbing this interaction lead to decreased tRNA stability. |
| doi_str_mv | 10.4161/rna.9.1.18009 |
| format | Article |
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Similar effect has been observed for pathogenic mutations in nuclear genes encoding mitochondrial aminoacyl-tRNA-synthetases, while over-expression of mitochondrial aminoacyl-tRNA synthetases or elongation factor EF-Tu rescued mutated tRNAs from degradation.
In this review we summarize experimental data concerning the possible regulatory mechanisms governing mitochondrial tRNA steady-state levels, and propose a hypothesis based on the tRNA channelling principle. According to this hypothesis, interaction of mitochondrial tRNA with proteins ensures not only tRNA synthesis, maturation and function, but also protection from degradation. Mutations perturbing this interaction lead to decreased tRNA stability.</description><identifier>ISSN: 1547-6286</identifier><identifier>EISSN: 1555-8584</identifier><identifier>DOI: 10.4161/rna.9.1.18009</identifier><identifier>PMID: 22258151</identifier><language>eng</language><publisher>United States: Taylor & Francis</publisher><subject>Amino Acyl-tRNA Synthetases - genetics ; Amino Acyl-tRNA Synthetases - metabolism ; aminoacyl-tRNA-synthetases ; Aminoacylation ; Binding ; Biology ; Bioscience ; Calcium ; Cancer ; Cell ; Cycle ; elongation factor Tu ; Genes, Mitochondrial ; Genome, Human ; human diseases ; Humans ; Landes ; mitochondria ; Mitochondria - enzymology ; Mitochondria - genetics ; Mitochondria - metabolism ; Mitochondrial Proteins - genetics ; Mitochondrial Proteins - metabolism ; Mutation ; Organogenesis ; Peptide Elongation Factor Tu - genetics ; Peptide Elongation Factor Tu - metabolism ; Polymorphism, Single Nucleotide ; Proteins ; RNA - genetics ; RNA - metabolism ; RNA Processing, Post-Transcriptional ; RNA Stability ; RNA, Transfer - genetics ; RNA, Transfer - metabolism ; Transcription, Genetic ; tRNA ; tRNA channelling</subject><ispartof>RNA biology, 2012-01, Vol.9 (1), p.33-39</ispartof><rights>Copyright © 2012 Landes Bioscience 2012</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c392t-89152e55ae89cb307d00623146b99f839d6e81f15c35e74145ef81e71c47d9c63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22258151$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Belostotsky, Ruth</creatorcontrib><creatorcontrib>Frishberg, Yaacov</creatorcontrib><creatorcontrib>Entelis, Nina</creatorcontrib><title>Human mitochondrial tRNA quality control in health and disease: A channelling mechanism?</title><title>RNA biology</title><addtitle>RNA Biol</addtitle><description>Mutations in human mitochondrial tRNA genes are associated with a number of multisystemic disorders. These single nucleotide substitutions in various domains of tRNA molecules may affect different steps of tRNA biogenesis. Often, the prominent decrease of aminoacylation and/or steady-state levels of affected mitochondrial tRNA have been demonstrated in patients' tissues and in cultured cells.
Similar effect has been observed for pathogenic mutations in nuclear genes encoding mitochondrial aminoacyl-tRNA-synthetases, while over-expression of mitochondrial aminoacyl-tRNA synthetases or elongation factor EF-Tu rescued mutated tRNAs from degradation.
In this review we summarize experimental data concerning the possible regulatory mechanisms governing mitochondrial tRNA steady-state levels, and propose a hypothesis based on the tRNA channelling principle. According to this hypothesis, interaction of mitochondrial tRNA with proteins ensures not only tRNA synthesis, maturation and function, but also protection from degradation. Mutations perturbing this interaction lead to decreased tRNA stability.</description><subject>Amino Acyl-tRNA Synthetases - genetics</subject><subject>Amino Acyl-tRNA Synthetases - metabolism</subject><subject>aminoacyl-tRNA-synthetases</subject><subject>Aminoacylation</subject><subject>Binding</subject><subject>Biology</subject><subject>Bioscience</subject><subject>Calcium</subject><subject>Cancer</subject><subject>Cell</subject><subject>Cycle</subject><subject>elongation factor Tu</subject><subject>Genes, Mitochondrial</subject><subject>Genome, Human</subject><subject>human diseases</subject><subject>Humans</subject><subject>Landes</subject><subject>mitochondria</subject><subject>Mitochondria - enzymology</subject><subject>Mitochondria - genetics</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondrial Proteins - genetics</subject><subject>Mitochondrial Proteins - metabolism</subject><subject>Mutation</subject><subject>Organogenesis</subject><subject>Peptide Elongation Factor Tu - genetics</subject><subject>Peptide Elongation Factor Tu - metabolism</subject><subject>Polymorphism, Single Nucleotide</subject><subject>Proteins</subject><subject>RNA - genetics</subject><subject>RNA - metabolism</subject><subject>RNA Processing, Post-Transcriptional</subject><subject>RNA Stability</subject><subject>RNA, Transfer - genetics</subject><subject>RNA, Transfer - metabolism</subject><subject>Transcription, Genetic</subject><subject>tRNA</subject><subject>tRNA channelling</subject><issn>1547-6286</issn><issn>1555-8584</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMFrFTEQhxdRbK0evcoevewzk02yyUWoRW3hYaG055CXzPoi2eQ12UXef2_qq89LoacZhm9-w3xN8x7IioGATzmalVrBCiQh6kVzCpzzTnLJXj70bOgEleKkeVPKL0J6IRV_3ZxQSrkEDqfN58tlMrGd_JzsNkWXvQntfPPjvL1fTPDzvrUpzjmF1sd2iybM29ZE1zpf0BR827waTSj47rGeNXffvt5eXHbr6-9XF-frzvaKzp1UwClyblAqu-nJ4AgRtAcmNkqNsldOoIQRuO05DgwYx1ECDmDZ4JQV_Vnz8ZC7y-l-wTLryReLIZiIaSka6vOcMiFURbsDanMqJeOod9lPJu8rpB-U6apMKw36r7LKf3iMXjYTuiP9z1EF5AGoxxyWjU_FeowWj2gNrNOQfu61ybO3AY_Z7JlVSgCq7S9X12sCRN3onRv_X_RxTHkyv1MOTs9mH1Ies4nWF90__c0fqrqgGA</recordid><startdate>20120101</startdate><enddate>20120101</enddate><creator>Belostotsky, Ruth</creator><creator>Frishberg, Yaacov</creator><creator>Entelis, Nina</creator><general>Taylor & Francis</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20120101</creationdate><title>Human mitochondrial tRNA quality control in health and disease</title><author>Belostotsky, Ruth ; Frishberg, Yaacov ; Entelis, Nina</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-89152e55ae89cb307d00623146b99f839d6e81f15c35e74145ef81e71c47d9c63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amino Acyl-tRNA Synthetases - genetics</topic><topic>Amino Acyl-tRNA Synthetases - metabolism</topic><topic>aminoacyl-tRNA-synthetases</topic><topic>Aminoacylation</topic><topic>Binding</topic><topic>Biology</topic><topic>Bioscience</topic><topic>Calcium</topic><topic>Cancer</topic><topic>Cell</topic><topic>Cycle</topic><topic>elongation factor Tu</topic><topic>Genes, Mitochondrial</topic><topic>Genome, Human</topic><topic>human diseases</topic><topic>Humans</topic><topic>Landes</topic><topic>mitochondria</topic><topic>Mitochondria - enzymology</topic><topic>Mitochondria - genetics</topic><topic>Mitochondria - metabolism</topic><topic>Mitochondrial Proteins - genetics</topic><topic>Mitochondrial Proteins - metabolism</topic><topic>Mutation</topic><topic>Organogenesis</topic><topic>Peptide Elongation Factor Tu - genetics</topic><topic>Peptide Elongation Factor Tu - metabolism</topic><topic>Polymorphism, Single Nucleotide</topic><topic>Proteins</topic><topic>RNA - genetics</topic><topic>RNA - metabolism</topic><topic>RNA Processing, Post-Transcriptional</topic><topic>RNA Stability</topic><topic>RNA, Transfer - genetics</topic><topic>RNA, Transfer - metabolism</topic><topic>Transcription, Genetic</topic><topic>tRNA</topic><topic>tRNA channelling</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Belostotsky, Ruth</creatorcontrib><creatorcontrib>Frishberg, Yaacov</creatorcontrib><creatorcontrib>Entelis, Nina</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>RNA biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Belostotsky, Ruth</au><au>Frishberg, Yaacov</au><au>Entelis, Nina</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human mitochondrial tRNA quality control in health and disease: A channelling mechanism?</atitle><jtitle>RNA biology</jtitle><addtitle>RNA Biol</addtitle><date>2012-01-01</date><risdate>2012</risdate><volume>9</volume><issue>1</issue><spage>33</spage><epage>39</epage><pages>33-39</pages><issn>1547-6286</issn><eissn>1555-8584</eissn><abstract>Mutations in human mitochondrial tRNA genes are associated with a number of multisystemic disorders. These single nucleotide substitutions in various domains of tRNA molecules may affect different steps of tRNA biogenesis. Often, the prominent decrease of aminoacylation and/or steady-state levels of affected mitochondrial tRNA have been demonstrated in patients' tissues and in cultured cells.
Similar effect has been observed for pathogenic mutations in nuclear genes encoding mitochondrial aminoacyl-tRNA-synthetases, while over-expression of mitochondrial aminoacyl-tRNA synthetases or elongation factor EF-Tu rescued mutated tRNAs from degradation.
In this review we summarize experimental data concerning the possible regulatory mechanisms governing mitochondrial tRNA steady-state levels, and propose a hypothesis based on the tRNA channelling principle. According to this hypothesis, interaction of mitochondrial tRNA with proteins ensures not only tRNA synthesis, maturation and function, but also protection from degradation. Mutations perturbing this interaction lead to decreased tRNA stability.</abstract><cop>United States</cop><pub>Taylor & Francis</pub><pmid>22258151</pmid><doi>10.4161/rna.9.1.18009</doi><tpages>7</tpages></addata></record> |
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| ispartof | RNA biology, 2012-01, Vol.9 (1), p.33-39 |
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| language | eng |
| recordid | cdi_landesbioscience_primary_rnabiology_article_18009 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Amino Acyl-tRNA Synthetases - genetics Amino Acyl-tRNA Synthetases - metabolism aminoacyl-tRNA-synthetases Aminoacylation Binding Biology Bioscience Calcium Cancer Cell Cycle elongation factor Tu Genes, Mitochondrial Genome, Human human diseases Humans Landes mitochondria Mitochondria - enzymology Mitochondria - genetics Mitochondria - metabolism Mitochondrial Proteins - genetics Mitochondrial Proteins - metabolism Mutation Organogenesis Peptide Elongation Factor Tu - genetics Peptide Elongation Factor Tu - metabolism Polymorphism, Single Nucleotide Proteins RNA - genetics RNA - metabolism RNA Processing, Post-Transcriptional RNA Stability RNA, Transfer - genetics RNA, Transfer - metabolism Transcription, Genetic tRNA tRNA channelling |
| title | Human mitochondrial tRNA quality control in health and disease: A channelling mechanism? |
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