Abstract
The 3' terminal nucleotide of turnip yellow mosaic virus (TYMV) RNA (23-25 S) may be esterified with valine in the presence of ATP and an enzyme preparation from Escherichia coli. The nucleotide composition near the valine-binding site is different for TYMV RNA and tRNA(Val) from cabbage, as shown by comparison of the valine adducts of nucleotides labeled with radioactive valine in T(1) RNase digests. Consequently, host tRNA(Val) is not involved in the observed charging of TYMV RNA with valine. The TYMV RNA appears to have a tRNA-like structure, at or near its 3' end, that is recognized by three different enzymes which specifically catalyze reactions involving tRNA.
MeSH Terms
Binding Sites
Carbon Isotopes
Esters
Nucleotides
Plant Viruses
RNA Nucleotidyltransferases
RNA, Transfer/analysis
RNA, Viral/analysis
Valine
Chemicals
Carbon Isotopes
Esters
Nucleotides
RNA, Viral
RNA, Transfer
RNA Nucleotidyltransferases
Valine
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Yot P
Pinck M
Haenni A L
Duranton H M
Chapeville F
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