Identification of an activity that interacts with the 3'-untranslated region of c-myc mRNA and the role of its target sequence in mediating rapid mRNA degradation.
Single or multiple copies of the pentameric motif, AUUUA, are found in the 3'-untranslated domain of most immediate early mRNAs. A broad body of data links this 5-base element to the selective degradation of these mRNAs. However, AUUUA motifs are neither always necessary nor always sufficient to tag an mRNA for rapid degradation. Here, we describe a cytoplasmic, protease-sensitive factor in Balb/c3T3 cells that interacts with the 3'-untranslated region of c-myc mRNA. The factor recognizes a 39-base uridine-rich domain adjacent to, but distinct from, the c-myc AUUUA motif. In chimeric mRNA constructs, the 39-base binding element cooperates with adjacent sequence material to destabilize beta-globin mRNA.
Alberta
J A
JA
Program in Cell and Developmental Biology, Harvard Medical School, Boston, Massachusetts 02115.
Rundell
K
K
Stiles
C D
CD
D016475:3T3 Cells; D000818:Animals; D001482:Base Composition; D001483:Base Sequence; D001665:Binding Sites; D003432:Cross-Linking Reagents; D005786:Gene Expression Regulation; D016259:Genes, myc; D051379:Mice; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000235:genetics* / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000378:metabolism*; D013329:Structure-Activity Relationship
D003432:Cross-Linking Reagents; D012333:RNA, Messenger; D016601:RNA-Binding Proteins