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rdf:type |
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lifeskim:mentions |
umls-concept:C0002520,
umls-concept:C0014834,
umls-concept:C0035711,
umls-concept:C0073243,
umls-concept:C0074289,
umls-concept:C0205161,
umls-concept:C0242767,
umls-concept:C0596311,
umls-concept:C1186763,
umls-concept:C1274040,
umls-concept:C1330957,
umls-concept:C1537998
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pubmed:issue |
24
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pubmed:dateCreated |
1989-2-23
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pubmed:databankReference |
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pubmed:abstractText |
The nucleotide sequence of the gene encoding the Escherichia coli selenocysteine tRNA (tRNA(SeCys] predicts an unusually long acceptor stem of 8 base pairs (one more than other tRNAs). Here we show by in vivo experiments (Northern blots, primer extension analysis) and by in vitro RNA processing studies that E. coli tRNA(SeCys) does contain this additional basepair, and that its formation results from abnormal cleavage by RNase P.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3062578-2423526,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3062578-2445614,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3062578-2447080,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3062578-2963962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3062578-2963963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3062578-3023854,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3062578-3033637,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3062578-3276688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3062578-3743551,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3062578-6197186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3062578-6300764
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acid-Specific,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease P,
http://linkedlifedata.com/resource/pubmed/chemical/ribonuclease P, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/tRNA, selenocysteine-
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0305-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11617-24
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:3062578-Base Composition,
pubmed-meshheading:3062578-Base Sequence,
pubmed-meshheading:3062578-Endoribonucleases,
pubmed-meshheading:3062578-Escherichia coli,
pubmed-meshheading:3062578-Escherichia coli Proteins,
pubmed-meshheading:3062578-Genes, Bacterial,
pubmed-meshheading:3062578-Molecular Sequence Data,
pubmed-meshheading:3062578-Nucleic Acid Conformation,
pubmed-meshheading:3062578-Protein Precursors,
pubmed-meshheading:3062578-RNA, Transfer, Amino Acid-Specific,
pubmed-meshheading:3062578-RNA Processing, Post-Transcriptional,
pubmed-meshheading:3062578-Ribonuclease P
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pubmed:year |
1988
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pubmed:articleTitle |
The unusually long amino acid acceptor stem of Escherichia coli selenocysteine tRNA results from abnormal cleavage by RNase P.
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pubmed:affiliation |
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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