| pubmed-article:3122828 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3122828 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:3122828 | lifeskim:mentions | umls-concept:C0024337 | lld:lifeskim |
| pubmed-article:3122828 | lifeskim:mentions | umls-concept:C0025653 | lld:lifeskim |
| pubmed-article:3122828 | lifeskim:mentions | umls-concept:C0039959 | lld:lifeskim |
| pubmed-article:3122828 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:3122828 | lifeskim:mentions | umls-concept:C2752192 | lld:lifeskim |
| pubmed-article:3122828 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:3122828 | lifeskim:mentions | umls-concept:C1511539 | lld:lifeskim |
| pubmed-article:3122828 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
| pubmed-article:3122828 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:3122828 | pubmed:dateCreated | 1988-3-18 | lld:pubmed |
| pubmed-article:3122828 | pubmed:abstractText | A new method has been developed to couple a lysine-reactive cross-linker to the 4-thiouridine residue at position 8 in the primary structure of the Escherichia coli initiator methionine tRNA (tRNAfMet). Incubation of the affinity-labeling tRNAfMet derivative with E. coli methionyl-tRNA synthetase (MetRS) yielded a covalent complex of the protein and nucleic acid and resulted in loss of amino acid acceptor activity of the enzyme. A stoichiometric relationship (1:1) was observed between the amount of cross-linked tRNA and the amount of enzyme inactivated. Cross-linking was effectively inhibited by unmodified tRNAfMet, but not by noncognate tRNAPhe. The covalent complex was digested with trypsin, and the resulting tRNA-bound peptides were purified from excess free peptides by anion-exchange chromatography. The tRNA was then degraded with T1 ribonuclease, and the peptides bound to the 4-thiouridine-containing dinucleotide were purified by high-pressure liquid chromatography. Two major peptide products were isolated plus several minor peptides. N-Terminal sequencing of the peptides obtained in highest yield revealed that the 4-thiouridine was cross-linked to lysine residues 402 and 439 in the primary sequence of MetRS. Since many prokaryotic tRNAs contain 4-thiouridine, the procedures described here should prove useful for identification of peptide sequences near this modified base when a variety of tRNAs are bound to specific proteins. | lld:pubmed |
| pubmed-article:3122828 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3122828 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3122828 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3122828 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3122828 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3122828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3122828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3122828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3122828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3122828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3122828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3122828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3122828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3122828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3122828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3122828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3122828 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3122828 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:3122828 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:3122828 | pubmed:author | pubmed-author:SchulmanL HLH | lld:pubmed |
| pubmed-article:3122828 | pubmed:author | pubmed-author:LenzRR | lld:pubmed |
| pubmed-article:3122828 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3122828 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:3122828 | pubmed:volume | 26 | lld:pubmed |
| pubmed-article:3122828 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3122828 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3122828 | pubmed:pagination | 7113-21 | lld:pubmed |
| pubmed-article:3122828 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:3122828 | pubmed:meshHeading | pubmed-meshheading:3122828-... | lld:pubmed |
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| pubmed-article:3122828 | pubmed:meshHeading | pubmed-meshheading:3122828-... | lld:pubmed |
| pubmed-article:3122828 | pubmed:meshHeading | pubmed-meshheading:3122828-... | lld:pubmed |
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| pubmed-article:3122828 | pubmed:meshHeading | pubmed-meshheading:3122828-... | lld:pubmed |
| pubmed-article:3122828 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3122828 | pubmed:articleTitle | Covalent coupling of 4-thiouridine in the initiator methionine tRNA to specific lysine residues in Escherichia coli methionyl-tRNA synthetase. | lld:pubmed |
| pubmed-article:3122828 | pubmed:affiliation | Department of Developmental Biology and Cancer, Albert Einstein College of Medicine, Bronx, New York 10461. | lld:pubmed |
| pubmed-article:3122828 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3122828 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3122828 | lld:pubmed |
