Purification and characterization of the Saccharomyces cerevisiae mitochondrial leucyl-tRNA synthetase
We have purified the product of the NAM2 gene, the mitochondrial leucyl-tRNA synthetase, from yeast mitochondria. The purified protein cross-reacts with antibodies raised against the product of a LacZ/NAM2 gene fusion and antibodies raised against the purified Escherichia coli leucyl-tRNA synthetase...
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| Veröffentlicht in: | The Journal of biological chemistry 1991-02, Vol.266 (4), p.2537-2541 |
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| container_issue | 4 |
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| container_title | The Journal of biological chemistry |
| container_volume | 266 |
| creator | ZAGORSKI, W CASTAING, B HERBERT, C. J LABOUESSE, M MARTIN, R SLONIMSKI, P. P |
| description | We have purified the product of the NAM2 gene, the mitochondrial leucyl-tRNA synthetase, from yeast mitochondria. The purified
protein cross-reacts with antibodies raised against the product of a LacZ/NAM2 gene fusion and antibodies raised against the
purified Escherichia coli leucyl-tRNA synthetase. The mass as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis
is about 100 kDa, consistent with the size predicted by the gene sequence (102 kDa). The N-terminal sequence of the protein
has been determined and shows that the first nine amino acids predicted by the gene sequence have been removed, probably during
transport into the mitochondria. |
| doi_str_mv | 10.1016/S0021-9258(18)52278-X |
| format | Article |
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protein cross-reacts with antibodies raised against the product of a LacZ/NAM2 gene fusion and antibodies raised against the
purified Escherichia coli leucyl-tRNA synthetase. The mass as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis
is about 100 kDa, consistent with the size predicted by the gene sequence (102 kDa). The N-terminal sequence of the protein
has been determined and shows that the first nine amino acids predicted by the gene sequence have been removed, probably during
transport into the mitochondria.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)52278-X</identifier><identifier>PMID: 1990003</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Adenosine Triphosphate - metabolism ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Blotting, Western ; Chromatography ; Cross Reactions ; Electrophoresis, Polyacrylamide Gel ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Genes, Fungal ; Hydrogen-Ion Concentration ; Kinetics ; Leucine - metabolism ; Leucine-tRNA Ligase - genetics ; Leucine-tRNA Ligase - immunology ; Leucine-tRNA Ligase - isolation & purification ; Leucine-tRNA Ligase - metabolism ; Life Sciences ; Ligases ; Mitochondria - enzymology ; Molecular Sequence Data ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Temperature</subject><ispartof>The Journal of biological chemistry, 1991-02, Vol.266 (4), p.2537-2541</ispartof><rights>1991 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357x-c2061fcf5da5db95bc70760e1d333199649b497afc890bf60885d9754ba7242c3</citedby><cites>FETCH-LOGICAL-c357x-c2061fcf5da5db95bc70760e1d333199649b497afc890bf60885d9754ba7242c3</cites><orcidid>0000-0001-5077-8978</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19545625$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1990003$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02141199$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>ZAGORSKI, W</creatorcontrib><creatorcontrib>CASTAING, B</creatorcontrib><creatorcontrib>HERBERT, C. J</creatorcontrib><creatorcontrib>LABOUESSE, M</creatorcontrib><creatorcontrib>MARTIN, R</creatorcontrib><creatorcontrib>SLONIMSKI, P. P</creatorcontrib><title>Purification and characterization of the Saccharomyces cerevisiae mitochondrial leucyl-tRNA synthetase</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We have purified the product of the NAM2 gene, the mitochondrial leucyl-tRNA synthetase, from yeast mitochondria. The purified
protein cross-reacts with antibodies raised against the product of a LacZ/NAM2 gene fusion and antibodies raised against the
purified Escherichia coli leucyl-tRNA synthetase. The mass as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis
is about 100 kDa, consistent with the size predicted by the gene sequence (102 kDa). The N-terminal sequence of the protein
has been determined and shows that the first nine amino acids predicted by the gene sequence have been removed, probably during
transport into the mitochondria.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Chromatography</subject><subject>Cross Reactions</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Fungal</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Leucine - metabolism</subject><subject>Leucine-tRNA Ligase - genetics</subject><subject>Leucine-tRNA Ligase - immunology</subject><subject>Leucine-tRNA Ligase - isolation & purification</subject><subject>Leucine-tRNA Ligase - metabolism</subject><subject>Life Sciences</subject><subject>Ligases</subject><subject>Mitochondria - enzymology</subject><subject>Molecular Sequence Data</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Temperature</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkd1u1DAQhS1EVZbCI1SKkED0IuCfOIkvV1WhlVYFUZD2zppMbGKUxMVOWpanr7dZFXxja-Y7Y_scQk4Z_cAoKz_eUMpZrris37P6THJe1fn2GVkxWotcSLZ9TlZPyAvyMsZfNK1CsWNyzJRKZ7Ei9uscnHUIk_NjBmObYQcBcDLB_V2K3mZTZ7IbwH3LDzs0MUMTzJ2LDkw2uMlj58c2OOiz3sy46_Pp2_U6i7sxKSeI5hU5stBH8_qwn5Afny6-n1_mmy-fr87XmxyFrP7kyGnJLFrZgmwbJRusaFVSw1ohRHpzWaimUBVYrBVtbEnrWraqkkUDFS84ihNytsztoNe3wQ0QdtqD05frjd7XkiEFS5PuWGLfLext8L9nEyc9uIim72E0fo6ayVpJqWgC5QJi8DEGY58mM6r3WejHLPTeaM1q_ZiF3ibd6eGCuRlM-0-1mJ_6bw99iAi9DTCii_9hspAll4l7c_iU-9ndu2B045LjZtC8LHWhE1KJB1Ezndo</recordid><startdate>19910205</startdate><enddate>19910205</enddate><creator>ZAGORSKI, W</creator><creator>CASTAING, B</creator><creator>HERBERT, C. 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P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357x-c2061fcf5da5db95bc70760e1d333199649b497afc890bf60885d9754ba7242c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Chromatography</topic><topic>Cross Reactions</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, Fungal</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Leucine - metabolism</topic><topic>Leucine-tRNA Ligase - genetics</topic><topic>Leucine-tRNA Ligase - immunology</topic><topic>Leucine-tRNA Ligase - isolation & purification</topic><topic>Leucine-tRNA Ligase - metabolism</topic><topic>Life Sciences</topic><topic>Ligases</topic><topic>Mitochondria - enzymology</topic><topic>Molecular Sequence Data</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>ZAGORSKI, W</creatorcontrib><creatorcontrib>CASTAING, B</creatorcontrib><creatorcontrib>HERBERT, C. J</creatorcontrib><creatorcontrib>LABOUESSE, M</creatorcontrib><creatorcontrib>MARTIN, R</creatorcontrib><creatorcontrib>SLONIMSKI, P. 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J</au><au>LABOUESSE, M</au><au>MARTIN, R</au><au>SLONIMSKI, P. P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of the Saccharomyces cerevisiae mitochondrial leucyl-tRNA synthetase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1991-02-05</date><risdate>1991</risdate><volume>266</volume><issue>4</issue><spage>2537</spage><epage>2541</epage><pages>2537-2541</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>We have purified the product of the NAM2 gene, the mitochondrial leucyl-tRNA synthetase, from yeast mitochondria. The purified
protein cross-reacts with antibodies raised against the product of a LacZ/NAM2 gene fusion and antibodies raised against the
purified Escherichia coli leucyl-tRNA synthetase. The mass as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis
is about 100 kDa, consistent with the size predicted by the gene sequence (102 kDa). The N-terminal sequence of the protein
has been determined and shows that the first nine amino acids predicted by the gene sequence have been removed, probably during
transport into the mitochondria.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1990003</pmid><doi>10.1016/S0021-9258(18)52278-X</doi><tpages>5</tpages><orcidid>https://orcid.org/0000-0001-5077-8978</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1991-02, Vol.266 (4), p.2537-2541 |
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| language | eng |
| recordid | cdi_hal_primary_oai_HAL_hal_02141199v1 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphate - metabolism Amino Acid Sequence Analytical, structural and metabolic biochemistry Biological and medical sciences Blotting, Western Chromatography Cross Reactions Electrophoresis, Polyacrylamide Gel Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Genes, Fungal Hydrogen-Ion Concentration Kinetics Leucine - metabolism Leucine-tRNA Ligase - genetics Leucine-tRNA Ligase - immunology Leucine-tRNA Ligase - isolation & purification Leucine-tRNA Ligase - metabolism Life Sciences Ligases Mitochondria - enzymology Molecular Sequence Data Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Temperature |
| title | Purification and characterization of the Saccharomyces cerevisiae mitochondrial leucyl-tRNA synthetase |
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