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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
1984-3-29
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pubmed:abstractText |
The mRNA capping reaction catalyzed by rat liver mRNA guanylyltransferase proceeds through an enzyme-GMP intermediate in which GMP is linked to the enzyme by a phosphoamide linkage. The studies described here show that GMP is bound to the epsilon-amino group of lysine of rat liver guanylyltransferase. The enzyme-[32P]GMP intermediate was digested with pronase to a [32P]GMP-peptide which was then converted to [32P]phosphoryl-peptide through periodate oxidation followed by beta-elimination. After alkaline hydrolysis of the [32P]phosphoryl-peptide, the major radioactive product co-electrophoresed with the authentic N epsilon-phospholysine on DEAE-cellulose paper. Neither [32P]Nimid-phosphohistidine nor Nguanido-phosphoarginine was detected in the hydrolysates. Furthermore, formation of N epsilon-guanylyl-lysine linkage on the enzyme was more directly shown by isolation of [32P]GMP(5' leads to N epsilon)lysine when the steps of periodate oxidation and beta-elimination were omitted. The results indicate that the nucleophile in the guanylyltransferase to which the guanylyl residue is linked is the epsilon-amino group of a lysine residue. [32P]Phosphoryl-lysine was also isolated from the vaccinia virus capping enzyme-[32P]GMP intermediate. Guanylyltransferase from HeLa cells, wheat germ, Artemia salina and yeast also formed the enzyme-GMP complex and, from the stability of the complex, the linkage between the enzyme and GMP was suggested to be a phosphoamide.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-1017010,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-10793698,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-1194286,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-13641241,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-291913,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-380639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-4910303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-4943553,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-5806584,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-6049515,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-6254974,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-6264433,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-6281766,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-6281779,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-6282835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-6290877,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-6301879,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-6329686,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-659428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-6933441,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-6985906,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6321153-7358712
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2195-201
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:6321153-5'-Guanylic Acid,
pubmed-meshheading:6321153-Animals,
pubmed-meshheading:6321153-Cell Nucleus,
pubmed-meshheading:6321153-Guanine Nucleotides,
pubmed-meshheading:6321153-Kinetics,
pubmed-meshheading:6321153-Liver,
pubmed-meshheading:6321153-Lysine,
pubmed-meshheading:6321153-Nucleotidyltransferases,
pubmed-meshheading:6321153-Phosphopeptides,
pubmed-meshheading:6321153-Phosphorus Radioisotopes,
pubmed-meshheading:6321153-Phosphorylation,
pubmed-meshheading:6321153-Protein Binding,
pubmed-meshheading:6321153-RNA Caps,
pubmed-meshheading:6321153-Rats
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pubmed:year |
1983
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pubmed:articleTitle |
Mechanism of the mRNA guanylyltransferase reaction: isolation of N epsilon-phospholysine and GMP (5' leads to N epsilon) lysine from the guanylyl-enzyme intermediate.
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pubmed:publicationType |
Journal Article
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