factor in serum and amniotic fluid is a substrate for the tRNA-modifying enzyme tRNA-guanine transferase
Q factor, a substance found in animal serum that enables cultured mammalian cells (L-M) to produce tRNA containing queuine (the base of ``nucleoside Q'', queuosine), has been purified to homogeneity from bovine amniotic fluid. Q factor causes the appearance of Q-containing tRNAAspin the L-...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1979-07, Vol.76 (7), p.3271-3275 |
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| creator | Katze, J.R Farkas, W.R |
| description | Q factor, a substance found in animal serum that enables cultured mammalian cells (L-M) to produce tRNA containing queuine (the base of ``nucleoside Q'', queuosine), has been purified to homogeneity from bovine amniotic fluid. Q factor causes the appearance of Q-containing tRNAAspin the L-M cells cultivated in serum-free medium, and this was used as an assay to monitor the purification of Q factor. Q factor is a competitive inhibitor of guanine for rabbit reticulocyte tRNA-guanine transferase, with a K1of 4.5 × 10-8M. Q factor is inactivated in both the L-M cell and tRNA-guanine transferase assays by treatment with periodate or cyanogen bromide, both of which react with queuine. In L-M cells, nearly complete conversion of Q-free to Q-containing tRNAAspis observed within 24 hr after addition of pure Q factor to the medium; actinomycin D, cycloheximide, and cycloleucine, inhibitors of RNA synthesis, protein synthesis, and nucleic acid methylation, respectively, do not inhibit this conversion. The product of the reaction, catalyzed by pure rabbit reticulocyte tRNA-guanine transferase, between Q factor and rabbit reticulocyte Q-free tRNAHisis chromatographically indistinguishable from Q-containing tRNAHis. |
| doi_str_mv | 10.1073/pnas.76.7.3271 |
| format | Article |
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Q factor causes the appearance of Q-containing tRNAAspin the L-M cells cultivated in serum-free medium, and this was used as an assay to monitor the purification of Q factor. Q factor is a competitive inhibitor of guanine for rabbit reticulocyte tRNA-guanine transferase, with a K1of 4.5 × 10-8M. Q factor is inactivated in both the L-M cell and tRNA-guanine transferase assays by treatment with periodate or cyanogen bromide, both of which react with queuine. In L-M cells, nearly complete conversion of Q-free to Q-containing tRNAAspis observed within 24 hr after addition of pure Q factor to the medium; actinomycin D, cycloheximide, and cycloleucine, inhibitors of RNA synthesis, protein synthesis, and nucleic acid methylation, respectively, do not inhibit this conversion. The product of the reaction, catalyzed by pure rabbit reticulocyte tRNA-guanine transferase, between Q factor and rabbit reticulocyte Q-free tRNAHisis chromatographically indistinguishable from Q-containing tRNAHis.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.76.7.3271</identifier><identifier>PMID: 291001</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amniotic fluid ; Amniotic Fluid - metabolism ; Animals ; Antimetabolites - pharmacology ; Cattle ; Cells, Cultured ; Chromatography ; Cultured cells ; Cyanogen Bromide - pharmacology ; Enzyme substrates ; Enzymes ; Female ; Guanine - metabolism ; Guanosine - analogs & derivatives ; Nucleic acids ; Nucleoside Q - blood ; Nucleoside Q - isolation & purification ; Nucleoside Q - metabolism ; Pregnancy ; Q factors ; Reticulocytes ; RNA, Transfer - metabolism ; Substrate Specificity ; Transfer RNA ; Transferases - metabolism ; Ungulates</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1979-07, Vol.76 (7), p.3271-3275</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3941-ad72ef0c8c5fd5d8179b8ae725301b4dc831d7a0027694d41e90e7d8cedb8a163</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/76/7.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/69972$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/69972$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/291001$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Katze, J.R</creatorcontrib><creatorcontrib>Farkas, W.R</creatorcontrib><title>factor in serum and amniotic fluid is a substrate for the tRNA-modifying enzyme tRNA-guanine transferase</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Q factor, a substance found in animal serum that enables cultured mammalian cells (L-M) to produce tRNA containing queuine (the base of ``nucleoside Q'', queuosine), has been purified to homogeneity from bovine amniotic fluid. Q factor causes the appearance of Q-containing tRNAAspin the L-M cells cultivated in serum-free medium, and this was used as an assay to monitor the purification of Q factor. Q factor is a competitive inhibitor of guanine for rabbit reticulocyte tRNA-guanine transferase, with a K1of 4.5 × 10-8M. Q factor is inactivated in both the L-M cell and tRNA-guanine transferase assays by treatment with periodate or cyanogen bromide, both of which react with queuine. In L-M cells, nearly complete conversion of Q-free to Q-containing tRNAAspis observed within 24 hr after addition of pure Q factor to the medium; actinomycin D, cycloheximide, and cycloleucine, inhibitors of RNA synthesis, protein synthesis, and nucleic acid methylation, respectively, do not inhibit this conversion. The product of the reaction, catalyzed by pure rabbit reticulocyte tRNA-guanine transferase, between Q factor and rabbit reticulocyte Q-free tRNAHisis chromatographically indistinguishable from Q-containing tRNAHis.</description><subject>Amniotic fluid</subject><subject>Amniotic Fluid - metabolism</subject><subject>Animals</subject><subject>Antimetabolites - pharmacology</subject><subject>Cattle</subject><subject>Cells, Cultured</subject><subject>Chromatography</subject><subject>Cultured cells</subject><subject>Cyanogen Bromide - pharmacology</subject><subject>Enzyme substrates</subject><subject>Enzymes</subject><subject>Female</subject><subject>Guanine - metabolism</subject><subject>Guanosine - analogs & derivatives</subject><subject>Nucleic acids</subject><subject>Nucleoside Q - blood</subject><subject>Nucleoside Q - isolation & purification</subject><subject>Nucleoside Q - metabolism</subject><subject>Pregnancy</subject><subject>Q factors</subject><subject>Reticulocytes</subject><subject>RNA, Transfer - metabolism</subject><subject>Substrate Specificity</subject><subject>Transfer RNA</subject><subject>Transferases - metabolism</subject><subject>Ungulates</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc2P1CAchonxa1y9ejAaOXlr_QFtgYOHzcavZKOJumfC8DHDpqUTaI3jXy9Nx8l68UTgeV4-XhB6TqAmwNnbQ9S55l3Na0Y5uYc2BCSpukbCfbQBoLwSDW0eoyc53wKAbAU8Qg-pJABkg_Zem2lMOEScXZoHrKPFeohhnILBvp-DxSFjjfO8zVPSk8O-6NPe4enbl8tqGG3wxxB32MXfx-G0upt1DLFMko7Zu6Sze4oeeN1n9-w0XqCbD-9_XH2qrr9-_Hx1eV0ZJhtSacup82CEab1trSBcboV2nLYMyLaxRjBiuV7e1cnGNsRJcNwK42zxSMcu0Lt138O8HZw1LpZL9OqQwqDTUY06qH9JDHu1G38qJpiAJV-veZPGnJPz5ygBtRSulsIV7xRXS-El8PLugWd9bbjgVye8xP7Cu_E3_-PKz30_uV9TEV-s4m0uH3Y2Oyk5LfD1Cr0eld6lkNXNd1qOBwpCgGjZH6kUqH0</recordid><startdate>19790701</startdate><enddate>19790701</enddate><creator>Katze, J.R</creator><creator>Farkas, W.R</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><scope>FBQ</scope><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>5PM</scope></search><sort><creationdate>19790701</creationdate><title>factor in serum and amniotic fluid is a substrate for the tRNA-modifying enzyme tRNA-guanine transferase</title><author>Katze, J.R ; Farkas, W.R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3941-ad72ef0c8c5fd5d8179b8ae725301b4dc831d7a0027694d41e90e7d8cedb8a163</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Amniotic fluid</topic><topic>Amniotic Fluid - metabolism</topic><topic>Animals</topic><topic>Antimetabolites - pharmacology</topic><topic>Cattle</topic><topic>Cells, Cultured</topic><topic>Chromatography</topic><topic>Cultured cells</topic><topic>Cyanogen Bromide - pharmacology</topic><topic>Enzyme substrates</topic><topic>Enzymes</topic><topic>Female</topic><topic>Guanine - metabolism</topic><topic>Guanosine - analogs & derivatives</topic><topic>Nucleic acids</topic><topic>Nucleoside Q - blood</topic><topic>Nucleoside Q - isolation & purification</topic><topic>Nucleoside Q - metabolism</topic><topic>Pregnancy</topic><topic>Q factors</topic><topic>Reticulocytes</topic><topic>RNA, Transfer - metabolism</topic><topic>Substrate Specificity</topic><topic>Transfer RNA</topic><topic>Transferases - metabolism</topic><topic>Ungulates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Katze, J.R</creatorcontrib><creatorcontrib>Farkas, W.R</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Katze, J.R</au><au>Farkas, W.R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>factor in serum and amniotic fluid is a substrate for the tRNA-modifying enzyme tRNA-guanine transferase</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1979-07-01</date><risdate>1979</risdate><volume>76</volume><issue>7</issue><spage>3271</spage><epage>3275</epage><pages>3271-3275</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Q factor, a substance found in animal serum that enables cultured mammalian cells (L-M) to produce tRNA containing queuine (the base of ``nucleoside Q'', queuosine), has been purified to homogeneity from bovine amniotic fluid. Q factor causes the appearance of Q-containing tRNAAspin the L-M cells cultivated in serum-free medium, and this was used as an assay to monitor the purification of Q factor. Q factor is a competitive inhibitor of guanine for rabbit reticulocyte tRNA-guanine transferase, with a K1of 4.5 × 10-8M. Q factor is inactivated in both the L-M cell and tRNA-guanine transferase assays by treatment with periodate or cyanogen bromide, both of which react with queuine. In L-M cells, nearly complete conversion of Q-free to Q-containing tRNAAspis observed within 24 hr after addition of pure Q factor to the medium; actinomycin D, cycloheximide, and cycloleucine, inhibitors of RNA synthesis, protein synthesis, and nucleic acid methylation, respectively, do not inhibit this conversion. The product of the reaction, catalyzed by pure rabbit reticulocyte tRNA-guanine transferase, between Q factor and rabbit reticulocyte Q-free tRNAHisis chromatographically indistinguishable from Q-containing tRNAHis.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>291001</pmid><doi>10.1073/pnas.76.7.3271</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1979-07, Vol.76 (7), p.3271-3275 |
| issn | 0027-8424 1091-6490 |
| language | eng |
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| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amniotic fluid Amniotic Fluid - metabolism Animals Antimetabolites - pharmacology Cattle Cells, Cultured Chromatography Cultured cells Cyanogen Bromide - pharmacology Enzyme substrates Enzymes Female Guanine - metabolism Guanosine - analogs & derivatives Nucleic acids Nucleoside Q - blood Nucleoside Q - isolation & purification Nucleoside Q - metabolism Pregnancy Q factors Reticulocytes RNA, Transfer - metabolism Substrate Specificity Transfer RNA Transferases - metabolism Ungulates |
| title | factor in serum and amniotic fluid is a substrate for the tRNA-modifying enzyme tRNA-guanine transferase |
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