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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1976-8-2
pubmed:abstractText
Inhibition of protein synthesis in relaxed control E. coli results in the formation of chromatographically unique isoacceptor species of phenylalanine tRNA. The genetic origin and some functional properties of the major unique species of tRNA (Phe) produced during leucine starvation were investigated. RNA:DNA hybridization analyses revealed that the normally occurring and major unique species of tRNA (Phe) are generated from DNA sequences which are identical or closely related and that there may be only one such sequence in the E. coli chromosome. Results from 32P pulse-chase experiments revealed that the unique tRNA (Phe) can be converted to a chromatographically normal form upon resumption of cell growth in fully supplemented medium. These findings, taken with earlier results which indicate that the unique species is not derived from preexisting, normally occurring species, indicate that the unique tRNA(Phe) is a modification-deficient form of the normal species. Comparative studies of the unique and normal phenylalanine tRNAs revealed that the unique species is aminoacylated at a much lower rate than the normal species and is only about 60% as efficient in a tRNA-dependent, poly(U)-directed protein synthesizing system.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1848-57
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Unique phenylalanine transfer ribonucleic acids in relaxed control Escherichia coli: genetic origin and some functional properties.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.