Purified lupus antigen La recognizes an oligouridylate stretch common to the 3' termini of RNA polymerase III transcripts
摘要:
The small ribonucleoproteins recognized by anti-La sera consist mainly of RNA polymerase III products complexed with an antigenic cellular protein of 50 kd. A biochemical procedure for purifying the La protein from HeLa cells is described. The interaction of the isolated protein with a collection of model tRNA precursors, generated by ligation of specific oligonucleotides to the 3′ terminus of yeast tRNA Phe, was studied. The most stable complexes are formed with adducts possessing three or four terminal uridylate residues. Addition of a terminal phosphate, fragmentation of the RNA, or substitution of other nucleotides reduce the affinity for the La protein. The preferred terminal sequence recognized and bound by La protein is homologous to the transcriptional termination signal for RNA polymerase III.
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关键词:
Hela Cells Humans Phosphates DNA-Directed RNA Polymerases RNA Polymerase III Ribonucleoproteins RNA, Transfer Oligonucleotides Oligoribonucleotides Uracil Nucleotides
DOI:
10.1016/0092-8674(84)90083-7
被引量:
年份:
1986
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