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PMID: 12192062 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

3' end processing of Drosophila melanogaster histone pre-mRNAs: requirement for phosphorylated Drosophila stem-loop binding protein and coevolution of the histone pre-mRNA processing system.

Molecular and cellular biology ·Vol. 22 ·No. 18 ·2002-09-00 ·Pages 6648-60

Dominski Z, Yang XC, Raska CS, Santiago C, Borchers CH, Duronio RJ, Marzluff WF

Abstract

Synthetic pre-mRNAs containing the processing signals encoded by Drosophila melanogaster histone genes undergo efficient and faithful endonucleolytic cleavage in nuclear extracts prepared from Drosophila cultured cells and 0- to 13-h-old embryos. Biochemical requirements for the in vitro cleavage are similar to those previously described for the 3' end processing of mammalian histone pre-mRNAs. Drosophila 3' end processing does not require ATP and occurs in the presence of EDTA. However, in contrast to mammalian processing, Drosophila processing generates the final product ending four nucleotides after the stem-loop. Cleavage of the Drosophila substrates is abolished by depleting the extract of the Drosophila stem-loop binding protein (dSLBP), indicating that both dSLBP and the stem-loop structure in histone pre-mRNA are essential components of the processing machinery. Recombinant dSLBP expressed in insect cells by using the baculovirus system efficiently complements the depleted extract. Only the RNA-binding domain plus the 17 amino acids at the C terminus of dSLBP are required for processing. The full-length dSLBP expressed in insect cells is quantitatively phosphorylated on four residues in the C-terminal region. Dephosphorylation of the recombinant dSLBP reduces processing activity. Human and Drosophila SLBPs are not interchangeable and strongly inhibit processing in the heterologous extracts. The RNA-binding domain of the dSLBP does not substitute for the RNA-binding domain of the human SLBP in histone pre-mRNA processing in mammalian extracts. In addition to the stem-loop structure and dSLBP, 3' processing in Drosophila nuclear extracts depends on the presence of a short stretch of purines located ca. 20 nucleotides downstream from the stem, and an Sm-reactive factor, most likely the Drosophila counterpart of vertebrate U7 snRNP.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Cell Nucleus/metabolism Drosophila Proteins Drosophila melanogaster/metabolism,physiology Histones/metabolism Mice Molecular Sequence Data Nuclear Proteins Phosphorylation Protein Binding Protein Isoforms Protein Structure, Tertiary RNA, Messenger/metabolism RNA-Binding Proteins/chemistry,physiology Recombinant Proteins/metabolism Sequence Homology, Nucleic Acid mRNA Cleavage and Polyadenylation Factors
Chemicals
Drosophila Proteins Histones Nuclear Proteins Protein Isoforms RNA, Messenger RNA-Binding Proteins Recombinant Proteins SLBP protein, Drosophila SLBP protein, human Slbp protein, mouse mRNA Cleavage and Polyadenylation Factors
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Dominski Zbigniew
Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, 27599, USA.
Yang Xiao-Cui
Raska Christy S
Santiago Carlos
Borchers Christoph H
Duronio Robert J
Marzluff William F
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/MCB.22.18.6648-6660.2002
Published
2002-09-00
Pages
6648-60
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC135633
Subset
IM
Grants
NIGMS NIH HHS · R01 GM058921 · United States
NIGMS NIH HHS · GM58921 · United States
External Links
PubMed source DOI: 10.1128/MCB.22.18.6648-6660.2002 PMC Full Text View journal details
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