Imaging

@article{,

title = {A histidine accepting tRNA-like fold at the 3'-end of satellite tobacco mosaic virus RNA},

author = {B Felden and C Florentz and A McPherson and R Giege},

url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8065897},

isbn = {8065897},

year  = {1994},

date = {1994-01-01},

journal = {Nucleic Acids Res},

volume = {22},

number = {15},

pages = {2882-2886},

abstract = {A model of secondary structure is proposed for the 3'-terminal sequence of the satellite tobacco mosaic virus (STMV) RNA on the basis of phylogenetic comparisons with tobacco mosaic virus (TMV) genomic RNA. Sequence homologies and compensatory base changes found between the two related viral RNAs imply that the 3'-end of STMV RNA folds into a tRNA-like domain similar to that found in the TMV RNA. Accordingly, functional assays showed that STMV RNA can be aminoacylated in vitro with histidine by yeast histidyl-tRNA synthetase to plateaus reaching 30%. Histidylation properties of STMV RNA were compared to those of TMV RNA and of a canonical yeast tRNA(His) transcript which both are chargeable to nearly 100% plateau levels. Kinetic data indicate an excellent catalytic efficiency of STMV RNA charging expressed as Vmax/Km ratio, quasi-equivalent to that of TMV RNA, and only 17-fold reduced as compared to that of the yeast tRNAHis transcript. Biological implications of the structural mimicry between the tRNA-like regions of TMV and STMV RNAs are discussed in the light of the relationships of a satellite virus with its helper virus. This is the first report on a chargeable tRNA-like structure at the 3'-end of a satellite virus RNA.},

note = {0305-1048 

Journal Article},

keywords = {Acylation  Base Sequence  Comparative Study  Histidine/*metabolism  Histidine-tRNA Ligase/metabolism  Kinetics  Molecular Sequence Data  *Nucleic Acid Conformation  Phylogeny  RNA, FLORENTZ, His/metabolism  RNA, Non-U.S. Gov't  Tobacco Mosaic Virus/*genetics, Transfer, Transfer/*chemistry  RNA, Unité ARN, Viral/*chemistry  Saccharomyces cerevisiae/enzymology  Sequence Homology  Support},

pubstate = {published},

tppubtype = {article}

}