5′ and 3′ end modifications of spliceosomal RNAs in Plasmodium falciparum
5′ caps provide recognition sequences for the nuclear import of snRNAs. The 5′ and 3′ ends of snRNAs were studied in Plasmodium falciparum with a modified adapter ligation method, which showed that 5′ ends of U1, U2, U4, U5 and U6 snRNAs are capped. In P. falciparum, the 3′ ends of U1, U2, U4 and U5...
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Veröffentlicht in: | Molecular biology reports 2010-04, Vol.37 (4), p.2125-2133 |
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description | 5′ caps provide recognition sequences for the nuclear import of snRNAs. The 5′ and 3′ ends of snRNAs were studied in Plasmodium falciparum with a modified adapter ligation method, which showed that 5′ ends of U1, U2, U4, U5 and U6 snRNAs are capped. In P. falciparum, the 3′ ends of U1, U2, U4 and U5 snRNAs have free hydroxyl groups whereas U6 snRNA has a blocked 3′ end. An immunoprecipitation assay for trimethyl guanosine caps shows that the cap structures of parasite U1-U5 snRNAs are hypermethylated while U6 snRNA may be γ-mono-methylated. Bioinformatics analysis of proteins involved in hypermethylation and trafficking of snRNAs indicates that the methyltransferase TGS1 is present in the P. falciparum genome. PfTGS1 is larger than its orthologs and may have transmembrane domains in the C-terminus. Surprisingly, the snRNA trafficking protein Snurportin is absent from the P. falciparum genome suggesting that reminiscent of yeast, parasite snRNAs may be retained in the nucleus. |
doi_str_mv | 10.1007/s11033-009-9682-4 |
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The 5′ and 3′ ends of snRNAs were studied in Plasmodium falciparum with a modified adapter ligation method, which showed that 5′ ends of U1, U2, U4, U5 and U6 snRNAs are capped. In P. falciparum, the 3′ ends of U1, U2, U4 and U5 snRNAs have free hydroxyl groups whereas U6 snRNA has a blocked 3′ end. An immunoprecipitation assay for trimethyl guanosine caps shows that the cap structures of parasite U1-U5 snRNAs are hypermethylated while U6 snRNA may be γ-mono-methylated. Bioinformatics analysis of proteins involved in hypermethylation and trafficking of snRNAs indicates that the methyltransferase TGS1 is present in the P. falciparum genome. PfTGS1 is larger than its orthologs and may have transmembrane domains in the C-terminus. Surprisingly, the snRNA trafficking protein Snurportin is absent from the P. falciparum genome suggesting that reminiscent of yeast, parasite snRNAs may be retained in the nucleus.</description><identifier>ISSN: 0301-4851</identifier><identifier>EISSN: 1573-4978</identifier><identifier>DOI: 10.1007/s11033-009-9682-4</identifier><identifier>PMID: 19669595</identifier><language>eng</language><publisher>Dordrecht: Dordrecht : Springer Netherlands</publisher><subject>Animal Anatomy ; Animal Biochemistry ; Animals ; Bioinformatics ; Biomedical and Life Sciences ; Blotting, Northern ; Databases, Genetic ; Eukaryotes ; Gene Expression Profiling ; Gene Expression Regulation, Developmental ; Histology ; Humans ; Life Cycle Stages ; Life Sciences ; Methyltransferases - metabolism ; Molecular biology ; Morphology ; Parasites ; Plasmodium falciparum ; Plasmodium falciparum - cytology ; Plasmodium falciparum - enzymology ; Plasmodium falciparum - genetics ; Plasmodium falciparum - growth & development ; Proteins ; Reverse Transcriptase Polymerase Chain Reaction ; Ribonucleic acid ; RNA ; RNA Processing, Post-Transcriptional ; RNA, Protozoan - genetics ; RNA, Protozoan - metabolism ; RNA, Small Nuclear - genetics ; RNA, Small Nuclear - metabolism ; Sequence Homology, Amino Acid ; Spliceosomes - genetics</subject><ispartof>Molecular biology reports, 2010-04, Vol.37 (4), p.2125-2133</ispartof><rights>Springer Science+Business Media B.V. 2009</rights><rights>Springer Science+Business Media B.V. 2010</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c426t-5174a3dabb04978720045e73f3e90da9277291afd1ee6db78bf751f0b65873ad3</citedby><cites>FETCH-LOGICAL-c426t-5174a3dabb04978720045e73f3e90da9277291afd1ee6db78bf751f0b65873ad3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11033-009-9682-4$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11033-009-9682-4$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>315,781,785,27926,27927,41490,42559,51321</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19669595$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bawankar, Praveen</creatorcontrib><creatorcontrib>Shaw, Philip J</creatorcontrib><creatorcontrib>Sardana, Richa</creatorcontrib><creatorcontrib>Babar, Prasad H</creatorcontrib><creatorcontrib>Patankar, Swati</creatorcontrib><title>5′ and 3′ end modifications of spliceosomal RNAs in Plasmodium falciparum</title><title>Molecular biology reports</title><addtitle>Mol Biol Rep</addtitle><addtitle>Mol Biol Rep</addtitle><description>5′ caps provide recognition sequences for the nuclear import of snRNAs. The 5′ and 3′ ends of snRNAs were studied in Plasmodium falciparum with a modified adapter ligation method, which showed that 5′ ends of U1, U2, U4, U5 and U6 snRNAs are capped. In P. falciparum, the 3′ ends of U1, U2, U4 and U5 snRNAs have free hydroxyl groups whereas U6 snRNA has a blocked 3′ end. An immunoprecipitation assay for trimethyl guanosine caps shows that the cap structures of parasite U1-U5 snRNAs are hypermethylated while U6 snRNA may be γ-mono-methylated. Bioinformatics analysis of proteins involved in hypermethylation and trafficking of snRNAs indicates that the methyltransferase TGS1 is present in the P. falciparum genome. PfTGS1 is larger than its orthologs and may have transmembrane domains in the C-terminus. Surprisingly, the snRNA trafficking protein Snurportin is absent from the P. falciparum genome suggesting that reminiscent of yeast, parasite snRNAs may be retained in the nucleus.</description><subject>Animal Anatomy</subject><subject>Animal Biochemistry</subject><subject>Animals</subject><subject>Bioinformatics</subject><subject>Biomedical and Life Sciences</subject><subject>Blotting, Northern</subject><subject>Databases, Genetic</subject><subject>Eukaryotes</subject><subject>Gene Expression Profiling</subject><subject>Gene Expression Regulation, Developmental</subject><subject>Histology</subject><subject>Humans</subject><subject>Life Cycle Stages</subject><subject>Life Sciences</subject><subject>Methyltransferases - metabolism</subject><subject>Molecular biology</subject><subject>Morphology</subject><subject>Parasites</subject><subject>Plasmodium falciparum</subject><subject>Plasmodium falciparum - cytology</subject><subject>Plasmodium falciparum - enzymology</subject><subject>Plasmodium falciparum - 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The 5′ and 3′ ends of snRNAs were studied in Plasmodium falciparum with a modified adapter ligation method, which showed that 5′ ends of U1, U2, U4, U5 and U6 snRNAs are capped. In P. falciparum, the 3′ ends of U1, U2, U4 and U5 snRNAs have free hydroxyl groups whereas U6 snRNA has a blocked 3′ end. An immunoprecipitation assay for trimethyl guanosine caps shows that the cap structures of parasite U1-U5 snRNAs are hypermethylated while U6 snRNA may be γ-mono-methylated. Bioinformatics analysis of proteins involved in hypermethylation and trafficking of snRNAs indicates that the methyltransferase TGS1 is present in the P. falciparum genome. PfTGS1 is larger than its orthologs and may have transmembrane domains in the C-terminus. Surprisingly, the snRNA trafficking protein Snurportin is absent from the P. falciparum genome suggesting that reminiscent of yeast, parasite snRNAs may be retained in the nucleus.</abstract><cop>Dordrecht</cop><pub>Dordrecht : Springer Netherlands</pub><pmid>19669595</pmid><doi>10.1007/s11033-009-9682-4</doi><tpages>9</tpages></addata></record> |
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subjects | Animal Anatomy Animal Biochemistry Animals Bioinformatics Biomedical and Life Sciences Blotting, Northern Databases, Genetic Eukaryotes Gene Expression Profiling Gene Expression Regulation, Developmental Histology Humans Life Cycle Stages Life Sciences Methyltransferases - metabolism Molecular biology Morphology Parasites Plasmodium falciparum Plasmodium falciparum - cytology Plasmodium falciparum - enzymology Plasmodium falciparum - genetics Plasmodium falciparum - growth & development Proteins Reverse Transcriptase Polymerase Chain Reaction Ribonucleic acid RNA RNA Processing, Post-Transcriptional RNA, Protozoan - genetics RNA, Protozoan - metabolism RNA, Small Nuclear - genetics RNA, Small Nuclear - metabolism Sequence Homology, Amino Acid Spliceosomes - genetics |
title | 5′ and 3′ end modifications of spliceosomal RNAs in Plasmodium falciparum |
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