Studies on the ability of norleucine to replace methionine in the initiation of protein synthesis in E. coli
It has been previously shown that norleucine can acylate both tRNA F Met and tRNA F Met and be converted to fNorleu-tRNA F Met. The present studies have compared the reactivity of fNorleu-tRNA F Met with fMet-tRNA F Met in various reactions associated with protein synthesis. No significant differenc...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1970-12, Vol.141 (2), p.525-532 |
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| container_end_page | 532 |
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| container_title | Archives of biochemistry and biophysics |
| container_volume | 141 |
| creator | Kerwar, S.S. Weissbach, Herbert |
| description | It has been previously shown that norleucine can acylate both tRNA
F
Met and tRNA
F
Met and be converted to fNorleu-tRNA
F
Met. The present studies have compared the reactivity of fNorleu-tRNA
F
Met with fMet-tRNA
F
Met in various reactions associated with protein synthesis. No significant differences were observed in the binding to ribosomes, reaction with puromycin, and deformylation reaction. However, unlike methionine, norleucine was not able to repress any of the enzymes involved in methionine synthesis. |
| doi_str_mv | 10.1016/0003-9861(70)90170-0 |
| format | Article |
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F
Met and tRNA
F
Met and be converted to fNorleu-tRNA
F
Met. The present studies have compared the reactivity of fNorleu-tRNA
F
Met with fMet-tRNA
F
Met in various reactions associated with protein synthesis. No significant differences were observed in the binding to ribosomes, reaction with puromycin, and deformylation reaction. However, unlike methionine, norleucine was not able to repress any of the enzymes involved in methionine synthesis.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(70)90170-0</identifier><identifier>PMID: 4925003</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Bacterial Proteins - biosynthesis ; Caproates - metabolism ; Caproates - pharmacology ; Carbon Isotopes ; Electrophoresis ; Enzyme Repression ; Escherichia coli - metabolism ; Folic Acid ; Formates - metabolism ; Hydro-Lyases - biosynthesis ; Methionine - biosynthesis ; Methionine - metabolism ; Oxidoreductases - biosynthesis ; Puromycin - metabolism ; Ribosomes - metabolism ; RNA, Transfer - metabolism ; Transferases - biosynthesis</subject><ispartof>Archives of biochemistry and biophysics, 1970-12, Vol.141 (2), p.525-532</ispartof><rights>1970</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c338t-bd48665c4311c8cf3ea2b319039fd5cc1c7bc613730b9210a72a75bafb27a3ae3</citedby><cites>FETCH-LOGICAL-c338t-bd48665c4311c8cf3ea2b319039fd5cc1c7bc613730b9210a72a75bafb27a3ae3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0003986170901700$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4925003$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kerwar, S.S.</creatorcontrib><creatorcontrib>Weissbach, Herbert</creatorcontrib><title>Studies on the ability of norleucine to replace methionine in the initiation of protein synthesis in E. coli</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>It has been previously shown that norleucine can acylate both tRNA
F
Met and tRNA
F
Met and be converted to fNorleu-tRNA
F
Met. The present studies have compared the reactivity of fNorleu-tRNA
F
Met with fMet-tRNA
F
Met in various reactions associated with protein synthesis. No significant differences were observed in the binding to ribosomes, reaction with puromycin, and deformylation reaction. However, unlike methionine, norleucine was not able to repress any of the enzymes involved in methionine synthesis.</description><subject>Bacterial Proteins - biosynthesis</subject><subject>Caproates - metabolism</subject><subject>Caproates - pharmacology</subject><subject>Carbon Isotopes</subject><subject>Electrophoresis</subject><subject>Enzyme Repression</subject><subject>Escherichia coli - metabolism</subject><subject>Folic Acid</subject><subject>Formates - metabolism</subject><subject>Hydro-Lyases - biosynthesis</subject><subject>Methionine - biosynthesis</subject><subject>Methionine - metabolism</subject><subject>Oxidoreductases - biosynthesis</subject><subject>Puromycin - metabolism</subject><subject>Ribosomes - metabolism</subject><subject>RNA, Transfer - metabolism</subject><subject>Transferases - biosynthesis</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1970</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1L7DAUhoNc0fHjHyhkddFFx5OmbdrNBRG_QHChrkOanuKRTjMmqTD_3tQZXN5V4Dzve5I8jJ0JWAoQ1RUAyKypK3Gh4LIBoSCDPbYQ0FQZyLr4wxa_kUN2FMIHgBBFlR-wg6LJy8QWbHiJU0cYuBt5fEduWhoobrjr-ej8gJOlEXl03ON6MBb5CuM7uXGe0rZCI0UyMQ3n1tq7iImEzZhgoDDHbpfcuoFO2H5vhoCnu_OYvd3dvt48ZE_P948310-ZlbKOWdsVdVWVtpBC2Nr2Ek3eStGAbPqutFZY1dpKSCWhbXIBRuVGla3p21wZaVAes7_bvekxnxOGqFcULA6DGdFNQdeglBRlnYLFNmi9C8Fjr9eeVsZvtAA9S9azQT0b1Ar0j2QNqXa-2z-1K-x-Szurif_bckyf_CL0OljC0WJHHm3UnaP_X_ANTmuMPA</recordid><startdate>197012</startdate><enddate>197012</enddate><creator>Kerwar, S.S.</creator><creator>Weissbach, Herbert</creator><general>Elsevier Inc</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>197012</creationdate><title>Studies on the ability of norleucine to replace methionine in the initiation of protein synthesis in E. coli</title><author>Kerwar, S.S. ; Weissbach, Herbert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c338t-bd48665c4311c8cf3ea2b319039fd5cc1c7bc613730b9210a72a75bafb27a3ae3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1970</creationdate><topic>Bacterial Proteins - biosynthesis</topic><topic>Caproates - metabolism</topic><topic>Caproates - pharmacology</topic><topic>Carbon Isotopes</topic><topic>Electrophoresis</topic><topic>Enzyme Repression</topic><topic>Escherichia coli - metabolism</topic><topic>Folic Acid</topic><topic>Formates - metabolism</topic><topic>Hydro-Lyases - biosynthesis</topic><topic>Methionine - biosynthesis</topic><topic>Methionine - metabolism</topic><topic>Oxidoreductases - biosynthesis</topic><topic>Puromycin - metabolism</topic><topic>Ribosomes - metabolism</topic><topic>RNA, Transfer - metabolism</topic><topic>Transferases - biosynthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kerwar, S.S.</creatorcontrib><creatorcontrib>Weissbach, Herbert</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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kerwar, S.S.</au><au>Weissbach, Herbert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Studies on the ability of norleucine to replace methionine in the initiation of protein synthesis in E. coli</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1970-12</date><risdate>1970</risdate><volume>141</volume><issue>2</issue><spage>525</spage><epage>532</epage><pages>525-532</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>It has been previously shown that norleucine can acylate both tRNA
F
Met and tRNA
F
Met and be converted to fNorleu-tRNA
F
Met. The present studies have compared the reactivity of fNorleu-tRNA
F
Met with fMet-tRNA
F
Met in various reactions associated with protein synthesis. No significant differences were observed in the binding to ribosomes, reaction with puromycin, and deformylation reaction. However, unlike methionine, norleucine was not able to repress any of the enzymes involved in methionine synthesis.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>4925003</pmid><doi>10.1016/0003-9861(70)90170-0</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 1970-12, Vol.141 (2), p.525-532 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80773158 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Bacterial Proteins - biosynthesis Caproates - metabolism Caproates - pharmacology Carbon Isotopes Electrophoresis Enzyme Repression Escherichia coli - metabolism Folic Acid Formates - metabolism Hydro-Lyases - biosynthesis Methionine - biosynthesis Methionine - metabolism Oxidoreductases - biosynthesis Puromycin - metabolism Ribosomes - metabolism RNA, Transfer - metabolism Transferases - biosynthesis |
| title | Studies on the ability of norleucine to replace methionine in the initiation of protein synthesis in E. coli |
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