ID sequence-binding protein factor complexed in ribonucleoprotein particles.
We analyzed brain extracts from fetal or adult mice with a 32P-labeled 5'-half fragment of identifier (ID) sequence in a gel mobility shift assay. Upon digestion of extracts with RNase A prior to the binding reactions, a protein factor(s) that specifically binds to the fragment was shown to appreciably increase in amount with either of the extracts. Furthermore, the binding was competed with single-stranded ID sequences. These observations suggest that the protein factor is capable of interacting with either the genes or their small RNA transcripts.
Anzai
K
K
Department of Biochemistry, College of Science and Technology, Nihon University, Tokyo, Japan.
Goto
S
S
D000818:Animals; D001923:Brain Chemistry; D004268:DNA-Binding Proteins; D006609:High Mobility Group Proteins; D051379:Mice; D012313:RNA / Q000032:analysis*; D015534:Trans-Activators; D014157:Transcription Factors / Q000032:analysis*; D029867:Xenopus Proteins
D004268:DNA-Binding Proteins; D006609:High Mobility Group Proteins; C081930:Tfam protein, mouse; D015534:Trans-Activators; D014157:Transcription Factors; C097078:XL-MTTFA protein, Xenopus; D029867:Xenopus Proteins; D012313:RNA