Endonucleolysis in the turnover of insulin-like growth factor II mRNA

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Standard

Endonucleolysis in the turnover of insulin-like growth factor II mRNA. / Nielsen, F C; Christiansen, Jan.

I: Journal of Biological Chemistry, Bind 267, Nr. 27, 1992, s. 19404-11.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Nielsen, FC & Christiansen, J 1992, 'Endonucleolysis in the turnover of insulin-like growth factor II mRNA', Journal of Biological Chemistry, bind 267, nr. 27, s. 19404-11.

APA

Nielsen, F. C., & Christiansen, J. (1992). Endonucleolysis in the turnover of insulin-like growth factor II mRNA. Journal of Biological Chemistry, 267(27), 19404-11.

Vancouver

Nielsen FC, Christiansen J. Endonucleolysis in the turnover of insulin-like growth factor II mRNA. Journal of Biological Chemistry. 1992;267(27):19404-11.

Author

Nielsen, F C ; Christiansen, Jan. / Endonucleolysis in the turnover of insulin-like growth factor II mRNA. I: Journal of Biological Chemistry. 1992 ; Bind 267, Nr. 27. s. 19404-11.

Bibtex

@article{e742ffb08c9f11de8bc9000ea68e967b,
title = "Endonucleolysis in the turnover of insulin-like growth factor II mRNA",
abstract = "The overlapping transcription units constituting the rat insulin-like growth factor II (IGF-II) locus generate multiple mRNAs by using different promoters. Three promoters have been identified, giving rise to 4.6-, 3.8-, and 3.6-kilobase mRNAs. The latter, originating from promoter P3, is the most abundant IGF-II mRNA in the rat liver cell-line BRL-3A. Moreover, a non-polyadenylated 1.2-kilobase (kb) transcript and a 1.8-kb tail fragment are prominent transcripts at steady-state. In this study, we show that the 1.8-kb tail fragment is uncapped and sediments as a 30 S ribonucleoprotein particle, and is thus not actively engaged in protein synthesis. In contrast, both the 3.6-kb mRNA and the 1.2-kb transcript cosediment with polysomes. In the presence of cytoplasmic extracts, the full-length 3.6-kb mRNA is cleaved into the 1.8-kb tail fragment and a similar-sized upstream fragment. The cleavage occurs between a putative hairpin and a phylogenetically conserved guanosine-rich region which forms a stable higher order RNA structure in the presence of K+. We suggest that endonucleolysis is the initial step in IGF-II mRNA decay and that this event may participate in the post-transcriptional regulation of IGF-II production.",
author = "Nielsen, {F C} and Jan Christiansen",
note = "Keywords: Animals; Base Sequence; Cell Compartmentation; Cells, Cultured; Hydrogen Bonding; Insulin-Like Growth Factor II; Molecular Sequence Data; Molecular Weight; Nucleic Acid Conformation; Nucleic Acid Precursors; Oligodeoxyribonucleotides; RNA Caps; RNA Processing, Post-Transcriptional; RNA, Messenger; Rats; Ribonuclease T1; Sequence Alignment",
year = "1992",
language = "English",
volume = "267",
pages = "19404--11",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "27",

}

RIS

TY - JOUR

T1 - Endonucleolysis in the turnover of insulin-like growth factor II mRNA

AU - Nielsen, F C

AU - Christiansen, Jan

N1 - Keywords: Animals; Base Sequence; Cell Compartmentation; Cells, Cultured; Hydrogen Bonding; Insulin-Like Growth Factor II; Molecular Sequence Data; Molecular Weight; Nucleic Acid Conformation; Nucleic Acid Precursors; Oligodeoxyribonucleotides; RNA Caps; RNA Processing, Post-Transcriptional; RNA, Messenger; Rats; Ribonuclease T1; Sequence Alignment

PY - 1992

Y1 - 1992

N2 - The overlapping transcription units constituting the rat insulin-like growth factor II (IGF-II) locus generate multiple mRNAs by using different promoters. Three promoters have been identified, giving rise to 4.6-, 3.8-, and 3.6-kilobase mRNAs. The latter, originating from promoter P3, is the most abundant IGF-II mRNA in the rat liver cell-line BRL-3A. Moreover, a non-polyadenylated 1.2-kilobase (kb) transcript and a 1.8-kb tail fragment are prominent transcripts at steady-state. In this study, we show that the 1.8-kb tail fragment is uncapped and sediments as a 30 S ribonucleoprotein particle, and is thus not actively engaged in protein synthesis. In contrast, both the 3.6-kb mRNA and the 1.2-kb transcript cosediment with polysomes. In the presence of cytoplasmic extracts, the full-length 3.6-kb mRNA is cleaved into the 1.8-kb tail fragment and a similar-sized upstream fragment. The cleavage occurs between a putative hairpin and a phylogenetically conserved guanosine-rich region which forms a stable higher order RNA structure in the presence of K+. We suggest that endonucleolysis is the initial step in IGF-II mRNA decay and that this event may participate in the post-transcriptional regulation of IGF-II production.

AB - The overlapping transcription units constituting the rat insulin-like growth factor II (IGF-II) locus generate multiple mRNAs by using different promoters. Three promoters have been identified, giving rise to 4.6-, 3.8-, and 3.6-kilobase mRNAs. The latter, originating from promoter P3, is the most abundant IGF-II mRNA in the rat liver cell-line BRL-3A. Moreover, a non-polyadenylated 1.2-kilobase (kb) transcript and a 1.8-kb tail fragment are prominent transcripts at steady-state. In this study, we show that the 1.8-kb tail fragment is uncapped and sediments as a 30 S ribonucleoprotein particle, and is thus not actively engaged in protein synthesis. In contrast, both the 3.6-kb mRNA and the 1.2-kb transcript cosediment with polysomes. In the presence of cytoplasmic extracts, the full-length 3.6-kb mRNA is cleaved into the 1.8-kb tail fragment and a similar-sized upstream fragment. The cleavage occurs between a putative hairpin and a phylogenetically conserved guanosine-rich region which forms a stable higher order RNA structure in the presence of K+. We suggest that endonucleolysis is the initial step in IGF-II mRNA decay and that this event may participate in the post-transcriptional regulation of IGF-II production.

M3 - Journal article

C2 - 1527060

VL - 267

SP - 19404

EP - 19411

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 27

ER -

ID: 13885701