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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

Thiophosphorylation of U1-70K protein inhibits pre-mRNA splicing

Article Abstract:

A study was conducted on the importance of phosphorylation of the 70K protein of the mammamlian U1 small nuclear ribonucleoprotein (snRNP) in pre-mRNA splicing. A thiophosphorylated product resistant to phosphatase dephosphorylation was produced by phosphorylating the protein with ATP or ATP-gammaS in vitro. Results revealed that mature spliceosomes were produced and extract splicing activity returned after U1 snRNPs with normal phosphorylated 70K protein were used to complement HeLa nuclear splicing extracts whose endogenous U1 snRNPs have been removed. Splicing was inhibited however, when thiophosphorylated snRNPs were employed.

Author: Luhrmann, Reinhard, Tazi, Jamal, Kornstadt, Ute, Rossi, Ferdinand, Jeanteur, Philippe, Cathala, Guy, Brunel, Claude
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
RNA splicing

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Devious devices of Salmonella

Article Abstract:

The enteric pathogenic bacterium Salmonella typhimurium infects epithelial cells by using the host cells' epidermal growth factor (EGF) receptors. J.E. Galan and colleagues have proved that this process of cell infection, also called parasite-specified endocytosis, is accompanied by the tyrosine phosphorylation of the EGF receptor. This research provides additional evidence that tyrosine phosphorylation is basic to host signal transduction and communication with the cytoskeleton.

Author: Portnoy, Daniel A., Smith, Gregory A.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
Infection, Physiological aspects, Epithelial cells, Epidermal growth factor, Epidermal growth factors, Salmonella typhimurium, Endocytosis

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Recurrence of a binding motif?

Article Abstract:

Analyses of the structures of the histidine-containing phosphocarrier protein (HPr), acylphosphatase (APt) and ribonucleoproteins (RNPs) show that these proteins share a conserved region with three antiparallel beta-strands and two alpha-helices. HPr, APt and RNPs are all involved in phosphate binding. Mutation analysis has identified the amino terminus of the first helix as the probable phosphate binding site of these proteins.

Author: Jones, David T., Pearl, Laurence H., Swindells, Mark B., Orengo, Christine A., Thornton, Janet M.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
Analysis, Structure-activity relationships (Biochemistry)

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Subjects list: Research, Proteins, Phosphorylation
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