|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5
|
|
pubmed:dateCreated |
1983-4-21
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
A novel mutation in the anticodon stem of E. coli tRNA1Tyrsu3+ (G43 to U43) has been characterized. The gene coding for the mutant tRNA, carried by phage phi 80DHA61.3 a derivative of phi 80psu3+su0, produces only 20% of mature suppressor tRNA as compared with phi 80psu3+. Both the mutant tRNA precursor and mature tRNA have an altered conformation. The precursor tRNA coded for by phi 80DHA61.3 is processed by RNase P more slowly than the su3+ precursor and does not form as stable an enzyme-substrate complex as does su3+ precursor. phi 80 DHA61.3 also contains a large deletion which begins in the spacer region between the su3+ gene and the su0- gene, extends through the su0- gene and includes most of the repeated region following the tRNA genes.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-10085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-1094468,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-1099453,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-1104100,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-13701658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-14263771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-329557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-345126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-4557059,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-4599596,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-4860476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-4866395,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-4905085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-4905086,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-4922220,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-4923867,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-4938965,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-5227669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-5643523,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-5663335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-6170979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-6183002,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-6246368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-6248430,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-6258859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-6281446,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-7011569,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-7034960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-787937,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6298744-958482
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anticodon,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Restriction Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Endoribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acyl,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease P,
http://linkedlifedata.com/resource/pubmed/chemical/Uracil,
http://linkedlifedata.com/resource/pubmed/chemical/ribonuclease P, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/tRNA, tyrosine-
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Mar
|
|
pubmed:issn |
0305-1048
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
11
|
|
pubmed:volume |
11
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1491-505
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:6298744-Anticodon,
pubmed-meshheading:6298744-Base Sequence,
pubmed-meshheading:6298744-Coliphages,
pubmed-meshheading:6298744-DNA Restriction Enzymes,
pubmed-meshheading:6298744-Endoribonucleases,
pubmed-meshheading:6298744-Escherichia coli,
pubmed-meshheading:6298744-Escherichia coli Proteins,
pubmed-meshheading:6298744-Genes, Bacterial,
pubmed-meshheading:6298744-Guanine,
pubmed-meshheading:6298744-Kinetics,
pubmed-meshheading:6298744-Mutation,
pubmed-meshheading:6298744-Nucleic Acid Conformation,
pubmed-meshheading:6298744-RNA, Transfer, Amino Acyl,
pubmed-meshheading:6298744-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:6298744-Ribonuclease P,
pubmed-meshheading:6298744-Uracil
|
|
pubmed:year |
1983
|
|
pubmed:articleTitle |
A G43 to U43 mutation in E. coli tRNAtyrsu3+ which affects processing by RNase P.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|
