title: The efficiency of 3'-end formation contributes to the relative levels of different histone mRNAs.
abstract: Sequences at both the 5' and 3' ends of mouse histone genes contribute to the expression of individual genes. The 3' sequences required for high expression of the mouse H2a-614 gene are the same as the sequences required for 3'-end formation. When these sequences were substituted for the 3' end of the poorly expressed H2a-291 gene, expression of the H2a-291 gene was increased fivefold. A 65-nucleotide fragment containing the H2a-614 3' processing signal increased expression of the H2a-291 gene when it was placed in the proper orientation downstream of the H2a-291 3' end. The only mRNAs that accumulated from this gene ended at the H2a-291 3' end, which suggests that the transcript is sequentially processed. In an in vitro processing system, the different histone 3' ends showed different processing efficiencies, which correlated with their expression in cells. These results suggest that the efficiency of processing is important in determining the steady-state levels of individual mouse histone mRNAs.
authors: Department of Chemistry, Florida State University, Tallahassee 32306.
authors: T J
authors: TJ
authors: Liu
authors: B J
authors: BJ
authors: Levine
authors: A I
authors: AI
authors: Skoultchi
authors: W F
authors: WF
authors: Marzluff
mesh_terms: D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D002478:Cells, Cultured; D003001:Cloning, Molecular; D004252:DNA Mutational Analysis; D005786:Gene Expression Regulation; D006657:Histones / Q000235:genetics*; D051379:Mice; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010957:Plasmids; D011061:Poly A / Q000378:metabolism; D012323:RNA Processing, Post-Transcriptional; D012333:RNA, Messenger / Q000032:analysis*; D012689:Sequence Homology, Nucleic Acid; D015719:Single-Strand Specific DNA and RNA Endonucleases
chemical_list: D006657:Histones; D012333:RNA, Messenger; D011061:Poly A; D015719:Single-Strand Specific DNA and RNA Endonucleases