Abstract:
:Xenopus laevis 5S rRNA isolated from 7S particles or transcribed in vitro is found to adopt two alternative conformations. These two conformers contain different structural elements within the major TF III A binding domain, which, when isolated as RNA fragments, still interact with the transcription factor. Chemical modification of easily accessible adenines in their N-1 position does not have any measurable effect on the binding of 5S rRNA to TF III A. These observations are in support of the idea that only a small amount of conserved sequence information is required for the binding of the transcription factor, whereas specific secondary structure features seem to be essential.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Pieler T,Guddat U,Oei SL,Erdmann VAdoi
10.1093/nar/14.15.6313subject
Has Abstractpub_date
1986-08-11 00:00:00pages
6313-26issue
15eissn
0305-1048issn
1362-4962journal_volume
14pub_type
杂志文章abstract::A repeated sequence element which is located about 200 nucleotides upstream from the protein-coding portion of the muscle actin gene (probably within a large 5' intron) in the genome of the sea urchin, Strongylocentrotus purpuratus has been characterized, and shown to contain the sequence features which indicate that ...
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