Cloning and expression in Escherichia coli of a yeast mannosyltransferase from the asparagine-linked glycosylation pathway.
J Biol Chem
; 259(1): 378-82, 1984 Jan 10.
Article
en En
| MEDLINE
| ID: mdl-6368538
ABSTRACT
The yeast Saccharomyces cerevisiae temperature-sensitive lethal mutant alg1-1, has been previously shown to lack the activity necessary for the addition of the first mannose residue in the synthesis of lipid-linked precursor oligosaccharide. The gene ALG1 has been cloned by complementation of the temperature-sensitive mutation alg1-1 with a total genomic DNA library. The original DNA fragment isolated was 11,300 base pairs and has been subcloned to a 1,500-base pair fragment which is still capable of complementing alg1-1. The gene ALG1 has been mapped on chromosome II at a distance of 2.1 map units from LYS2. The ALG1 gene product has been shown to catalyze the transfer of a mannosyl residue from GDP-mannose to the lipid-linked acceptor GlcNAc2, yielding Man beta 1-4GlcNAc2-lipid, in lysates from Escherichia coli transformants. This result proves that ALG1 is the structural gene for the first mannosyltransferase in lipid-linked oligosaccharide assembly.
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Banco de datos:
MEDLINE
Asunto principal:
Asparagina
/
Saccharomyces cerevisiae
/
Clonación Molecular
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Escherichia coli
/
Hexosiltransferasas
/
Manosiltransferasas
Idioma:
En
Año:
1984
Tipo del documento:
Article