Initiation of translation at a UAG stop codon in the aldolase gene of Plasmodium falciparum

The gene coding for the key glycolytic enzyme fructose‐1,6‐diphosphate aldolase of the human malaria parasite Plasmodium falciparum lacks a functional AUG initiation codon for translation. Protein sequences of natural or in vitro translated aldolase include the candidate start methionine residue at...

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Bibliographic Details
Published in:The EMBO journal 1990-05, Vol.9 (5), p.1645-1649
Main Authors: Ghersa, P., Shrivastava, I.K., Perrin, L.H., Döbeli, H., Becherer, D.J., Matile, H., Meier, B., Certa, U.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Biological and medical sciences
Codon - genetics
Fructose-Bisphosphate Aldolase - genetics
Fundamental and applied biological sciences. Psychology
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Nucleic Acid Conformation
Plasmodium falciparum - enzymology
Plasmodium falciparum - genetics
Protein Biosynthesis - genetics
Reticulocytes - metabolism
RNA, Messenger - genetics
Terminator Regions, Genetic - genetics
Translation. Translation factors. Protein processing
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Summary:The gene coding for the key glycolytic enzyme fructose‐1,6‐diphosphate aldolase of the human malaria parasite Plasmodium falciparum lacks a functional AUG initiation codon for translation. Protein sequences of natural or in vitro translated aldolase include the candidate start methionine residue at internal positions. No additional AUG start codon is found in genomic DNA, cDNA or mRNA sequences. Instead, a UAG chain termination codon is recognized as the start signal of protein synthesis in vivo and in vitro.
ISSN:0261-4189
1460-2075
DOI:10.1002/j.1460-2075.1990.tb08284.x