Structure of the amino-terminal end of mammalian elongation factor Tu
Mixed sequence oligonucleotide probes complementary for peptides Thr-Ile-Glu-Lys-Phe-Glu and Asp-Tyr-Val-Lys-Asn-Met-Ile which are located in the amino-terminal region of eEF-Tu were used to obtain reverse transcripts from murine and human poly(A) super(+) mRNA. Reverse transcription products were s...
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| Veröffentlicht in: | Nucleic acids research 1986-03, Vol.14 (5), p.2409-2409 |
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| creator | RAO, T. R SLOBIN, L. I |
| description | Mixed sequence oligonucleotide probes complementary for peptides Thr-Ile-Glu-Lys-Phe-Glu and Asp-Tyr-Val-Lys-Asn-Met-Ile which are located in the amino-terminal region of eEF-Tu were used to obtain reverse transcripts from murine and human poly(A) super(+) mRNA. Reverse transcription products were separated on polyacrylamide gels and sequenced. Both sequences contain an open reading frame of 282 nucleotides which code for the same sequence of ninety-four amino acids including the start methionine (ATG) codon. A comparison of this amino acid sequence with those reported for yeast and Artemia) eEF-Tu indicated only three differences between the brine shrimp and mammals only seven between yeast and mammals (see Fig. 1). |
| doi_str_mv | 10.1093/nar/14.5.2409 |
| format | Article |
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R ; SLOBIN, L. I</creator><creatorcontrib>RAO, T. R ; SLOBIN, L. I</creatorcontrib><description>Mixed sequence oligonucleotide probes complementary for peptides Thr-Ile-Glu-Lys-Phe-Glu and Asp-Tyr-Val-Lys-Asn-Met-Ile which are located in the amino-terminal region of eEF-Tu were used to obtain reverse transcripts from murine and human poly(A) super(+) mRNA. Reverse transcription products were separated on polyacrylamide gels and sequenced. Both sequences contain an open reading frame of 282 nucleotides which code for the same sequence of ninety-four amino acids including the start methionine (ATG) codon. A comparison of this amino acid sequence with those reported for yeast and Artemia) eEF-Tu indicated only three differences between the brine shrimp and mammals only seven between yeast and mammals (see Fig. 1).</description><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/14.5.2409</identifier><identifier>PMID: 3960725</identifier><identifier>CODEN: NARHAD</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Biological and medical sciences ; DNA ; elongation factor Tu ; Fundamental and applied biological sciences. Psychology ; Humans ; Mice ; Molecular and cellular biology ; Molecular genetics ; mRNA ; nucleotide sequence ; Peptide Elongation Factors ; reverse transcription ; Sequence Homology, Nucleic Acid ; Translation. Translation factors. 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R</creatorcontrib><creatorcontrib>SLOBIN, L. I</creatorcontrib><title>Structure of the amino-terminal end of mammalian elongation factor Tu</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>Mixed sequence oligonucleotide probes complementary for peptides Thr-Ile-Glu-Lys-Phe-Glu and Asp-Tyr-Val-Lys-Asn-Met-Ile which are located in the amino-terminal region of eEF-Tu were used to obtain reverse transcripts from murine and human poly(A) super(+) mRNA. Reverse transcription products were separated on polyacrylamide gels and sequenced. Both sequences contain an open reading frame of 282 nucleotides which code for the same sequence of ninety-four amino acids including the start methionine (ATG) codon. A comparison of this amino acid sequence with those reported for yeast and Artemia) eEF-Tu indicated only three differences between the brine shrimp and mammals only seven between yeast and mammals (see Fig. 1).</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>DNA</subject><subject>elongation factor Tu</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Mice</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>mRNA</subject><subject>nucleotide sequence</subject><subject>Peptide Elongation Factors</subject><subject>reverse transcription</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Translation. Translation factors. Protein processing</subject><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkL1PwzAUxC0EKqUwMiJlQGxp_RnHAwOqyodUiYEyRy-xU4wSuzgOEv89qYgqmJhu-N093TuELgmeE6zYwkFYED4Xc8qxOkJTwjKacpXRYzTFDIuUYJ6forOue8eYcCL4BE2YyrCkYopWLzH0VeyDSXydxDeTQGudT6MJg0KTGKf3pIW2hcaCS0zj3Rai9S6poYo-JJv-HJ3U0HTmYtQZer1fbZaP6fr54Wl5t053VNCYaoNFLbRmrMYaMsw4r6mEMidUG1XlstRUc61AcUzznHHIRUY0lSLHrCwJm6Hbn7u7vmyNroyLAZpiF2wL4avwYIu_xNm3Yus_CzY8nOVD_mbMB__Rmy4Wre0q0zTgjO-7QmZSCi7-NxKeEUrl3nj1u9GhyjjwwK9HDl0FTR3AVbY72KSSjDLFvgE27Ipl</recordid><startdate>19860311</startdate><enddate>19860311</enddate><creator>RAO, T. R</creator><creator>SLOBIN, L. I</creator><general>Oxford University Press</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19860311</creationdate><title>Structure of the amino-terminal end of mammalian elongation factor Tu</title><author>RAO, T. R ; SLOBIN, L. I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p252t-de05f5dd33f0da60344f27ab812de9c87bd2d4d9a94028834a8561d275803bb13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>DNA</topic><topic>elongation factor Tu</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Mice</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>mRNA</topic><topic>nucleotide sequence</topic><topic>Peptide Elongation Factors</topic><topic>reverse transcription</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Translation. Translation factors. Protein processing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>RAO, T. R</creatorcontrib><creatorcontrib>SLOBIN, L. I</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>RAO, T. R</au><au>SLOBIN, L. I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure of the amino-terminal end of mammalian elongation factor Tu</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>1986-03-11</date><risdate>1986</risdate><volume>14</volume><issue>5</issue><spage>2409</spage><epage>2409</epage><pages>2409-2409</pages><issn>0305-1048</issn><eissn>1362-4962</eissn><coden>NARHAD</coden><abstract>Mixed sequence oligonucleotide probes complementary for peptides Thr-Ile-Glu-Lys-Phe-Glu and Asp-Tyr-Val-Lys-Asn-Met-Ile which are located in the amino-terminal region of eEF-Tu were used to obtain reverse transcripts from murine and human poly(A) super(+) mRNA. Reverse transcription products were separated on polyacrylamide gels and sequenced. Both sequences contain an open reading frame of 282 nucleotides which code for the same sequence of ninety-four amino acids including the start methionine (ATG) codon. A comparison of this amino acid sequence with those reported for yeast and Artemia) eEF-Tu indicated only three differences between the brine shrimp and mammals only seven between yeast and mammals (see Fig. 1).</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><pmid>3960725</pmid><doi>10.1093/nar/14.5.2409</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0305-1048 |
| ispartof | Nucleic acids research, 1986-03, Vol.14 (5), p.2409-2409 |
| issn | 0305-1048 1362-4962 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_339668 |
| source | MEDLINE; Oxford University Press Archive; PubMed Central |
| subjects | Amino Acid Sequence Animals Base Sequence Biological and medical sciences DNA elongation factor Tu Fundamental and applied biological sciences. Psychology Humans Mice Molecular and cellular biology Molecular genetics mRNA nucleotide sequence Peptide Elongation Factors reverse transcription Sequence Homology, Nucleic Acid Translation. Translation factors. Protein processing |
| title | Structure of the amino-terminal end of mammalian elongation factor Tu |
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