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PMID: 1757461 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Isolation, characterization, and expression of cDNAs encoding murine alpha-mannosidase II, a Golgi enzyme that controls conversion of high mannose to complex N-glycans.

The Journal of cell biology ·Vol. 115 ·No. 6 ·1991-12-00 ·Pages 1521-34

Moremen KW, Robbins PW

Abstract

Golgi alpha-mannosidase II (GlcNAc transferase I-dependent alpha 1,3[alpha 1,6] mannosidase, EC 3.2.1.114) catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures. We have isolated overlapping clones from a murine cDNA library encoding the full length alpha-mannosidase II open reading frame and most of the 5' and 3' untranslated region. The coding sequence predicts a type II transmembrane protein with a short cytoplasmic tail (five amino acids), a single transmembrane domain (21 amino acids), and a large COOH-terminal catalytic domain (1,124 amino acids). This domain organization which is shared with the Golgi glycosyl-transferases suggests that the common structural motifs may have a functional role in Golgi enzyme function or localization. Three sets of polyadenylated clones were isolated extending 3' beyond the open reading frame by as much as 2,543 bp. Northern blots suggest that these polyadenylated clones totaling 6.1 kb in length correspond to minor message species smaller than the full length message. The largest and predominant message on Northern blots (7.5 kb) presumably extends another approximately 1.4-kb downstream beyond the longest of the isolated clones. Transient expression of the alpha-mannosidase II cDNA in COS cells resulted in 8-12-fold overexpression of enzyme activity, and the appearance of cross-reactive material in a perinuclear membrane array consistent with a Golgi localization. A region within the catalytic domain of the alpha-mannosidase II open reading frame bears a strong similarity to a corresponding sequence in the rat liver endoplasmic reticulum alpha-mannosidase and the vacuolar alpha-mannosidase of Saccharomyces cerevisiae. Partial human alpha-mannosidase II cDNA clones were also isolated and the gene was localized to human chromosome 5.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Cell Line Chromosome Mapping Chromosomes, Human, Pair 5 Cloning, Molecular DNA/isolation & purification,metabolism Fluorescent Antibody Technique Golgi Apparatus/enzymology Humans Male Mannose/metabolism Mannosidases/genetics,metabolism Mice Molecular Sequence Data Open Reading Frames Organ Specificity/genetics Polysaccharides/metabolism Rats Restriction Mapping Sequence Alignment Transfection
Chemicals
Polysaccharides DNA Mannosidases mannosyl-oligosaccharide 1,3 - 1,6-alpha-mannosidase Mannose
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Moremen K W
Center for Cancer Research, Massachusetts Institute of Technology, Cambridge 02139.
Robbins P W
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.115.6.1521
Published
1991-12-00
Pages
1521-34
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2289207
Subset
IM
Grants
NCI NIH HHS · CA14051 · United States
NCI NIH HHS · CA26712 · United States
NIGMS NIH HHS · GM31318 · United States
Databases
GENBANK
M60692, M60693, M60694, M60695, M60696, M60697, S66758, S66760, S66765, S73487, X61172
External Links
PubMed source DOI: 10.1083/jcb.115.6.1521 PMC Full Text View journal details
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