Identification of the human U7 snRNP as one of several factors involved in the 3' end maturation of histone premessenger RNA's.
In eukaryotic cells, the conversion of gene transcripts into messenger RNA's involves multiple factors, including the highly abundant small nuclear ribonucleoprotein (snRNP) complexes that mediate the splicing reaction. Separable factors are also required for the 3' end processing of histone pre-mRNA's. The two conserved signals flanking the 3' cleavage site are recognized by discrete components present in active HeLa cell extracts: the upstream stem loop associates with a nuclease-insensitive factor, while binding to the downstream element is mediated by a component having the properties of a snRNP. The sequence of the RNA moiety of the low abundance human U7 snRNP suggests how the relatively degenerate downstream element of mammalian pre-mRNA's could be recognized by RNA base-pairing.
Mowry
K L
KL
Howard Hughes Medical Institute, Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06510.
Steitz
J A
JA
D001483:Base Sequence; D004722:Endoribonucleases; D006367:HeLa Cells / Q000378:metabolism; D006657:Histones / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D012322:RNA Precursors / Q000235:genetics*; D012323:RNA Processing, Post-Transcriptional; D016914:Ribonuclease H; D012261:Ribonucleoproteins / Q000235:genetics*; D017411:Ribonucleoproteins, Small Nuclear
D006657:Histones; D012322:RNA Precursors; D012261:Ribonucleoproteins; D017411:Ribonucleoproteins, Small Nuclear; D004722:Endoribonucleases; D016914:Ribonuclease H