Novel metabolism of several beta zero-thalassemic beta-globin mRNAs in the erythroid tissues of transgenic mice.
Journal Title: EMBO Journal - Year 1989, Vol 8, Issue 9
Abstract
Mice that are transgenic for human beta zero-thalassemic beta-globin alleles were generated in order to study how beta zero-thalassemic mutations affect beta-globin RNA metabolism in erythroid tissues. Three thalassemic alleles were studied, each of which harbors either a frameshift or a nonsense mutation. These mutations result in the premature termination of beta-globin mRNA translation and an abnormally low level of beta-globin mRNA in the peripheral blood of thalassemic patients. Comparative studies of mice that express any of the beta zero-thalassemic transgenes with mice that express a normal human beta-globin transgene demonstrated that all three thalassemic mRNAs are metabolized in erythroid tissues abnormally. RNA blotting and S1 nuclease transcript mapping revealed for each thalassemic transgene that (i) the full-length mRNA is abnormally short-lived and (ii) in addition to full-length mRNA, three more stable yet smaller RNAs are present. These smaller RNAs are polyadenylated and lack the mRNA 5' end.
Authors and Affiliations
S Lim, J J Mullins, C M Chen, K W Gross, L E Maquat
Keywords
Related Articles
- EP ID EP84135
- DOI -
- Views 33
- Downloads 0
Ca(2+) signalling is not required for chemotaxis in Dictyostelium.
Dictyostelium cells can move rapidly towards a source of cyclic-AMP (cAMP). This chemoattractant is detected by G-protein-linked receptors, which trigger a signalling cascade including a rapid influx of Ca(2+). We have d...
Novel metabolism of several beta zero-thalassemic beta-globin mRNAs in the erythroid tissues of transgenic mice.
Mice that are transgenic for human beta zero-thalassemic beta-globin alleles were generated in order to study how beta zero-thalassemic mutations affect beta-globin RNA metabolism in erythroid tissues. Three thalassemic...
Dimeric arrangement and structure of the membrane-bound acetylcholine receptor studied by electron microscopy.
The acetylcholine receptor protein (AChR) from the electric organ of Torpedo marmorata is studied in its membrane-bound form by electron microscopy and single-particle image averaging. About half the molecule protrudes f...