Linked Life Data

1532576

Source:http://linkedlifedata.com/resource/pubmed/id/1532576

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1992-5-4
pubmed:abstractText
To study the sorting of proteins in Dictyostelium discoideum, we used vector constructs that contain cDNA coding for the entire beta-hexosaminidase protein to prepare transformants of a mutant that lacks this enzyme activity. These transformants overexpressed active, normally processed beta-hexosaminidase. The overexpressed enzyme colocalized with other acid hydrolases in the soluble fraction of vesicles in the lysosomal region of Percoll gradients. The sorting of other hydrolases was unaltered. We also prepared transformants with constructs that contain 22 (Hex 22-Inv), 70 (Hex 70-Inv), and 532 (Hex 532-Inv) amino-terminal amino acids from beta-hexosaminidase fused in frame with the coding sequence for the yeast SUC2 gene product, invertase. Fusion molecular masses were those expected for fully N-glycosylated proteins. Hex 22-Inv was rapidly (t1/2 less than 30 min) and quantitatively secreted. The others were slowly (t1/2 greater than 5 h) and partially secreted. Each expressed invertase activity. During growth, the invertase activity of Hex 70-Inv and Hex 532-Inv was retained to the same extent as that of endogenous lysosomal enzymes. Most of the Hex 70-Inv migrated in Percoll gradients with vesicles of intermediate density (d = 1.055), but a portion co-migrated with lysosomal enzymes at d = 1.08. Hex 70-Inv was sulfated, and its N-glycosides were resistant to endoglycosidase H, indicating Golgi processing. Hex 70-Inv and Hex 532-Inv, like endogenous lysosomal enzymes, were subject to developmentally induced secretion.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
267
pubmed:geneSymbol
SUC2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5942-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:1532576-Animals, pubmed-meshheading:1532576-Base Sequence, pubmed-meshheading:1532576-Cell Fractionation, pubmed-meshheading:1532576-Dictyostelium, pubmed-meshheading:1532576-Genetic Vectors, pubmed-meshheading:1532576-Glycoside Hydrolases, pubmed-meshheading:1532576-Glycosylation, pubmed-meshheading:1532576-Kinetics, pubmed-meshheading:1532576-Lysosomes, pubmed-meshheading:1532576-Molecular Sequence Data, pubmed-meshheading:1532576-Molecular Weight, pubmed-meshheading:1532576-Oligodeoxyribonucleotides, pubmed-meshheading:1532576-Plasmids, pubmed-meshheading:1532576-Protein Processing, Post-Translational, pubmed-meshheading:1532576-Recombinant Fusion Proteins, pubmed-meshheading:1532576-Saccharomyces cerevisiae, pubmed-meshheading:1532576-Subcellular Fractions, pubmed-meshheading:1532576-beta-Fructofuranosidase, pubmed-meshheading:1532576-beta-N-Acetylhexosaminidases
pubmed:year
1992
pubmed:articleTitle
A sequence in beta-hexosaminidase from Dictyostelium discoideum required for sorting of proteins to a compartment involved in developmentally induced secretion.
pubmed:affiliation
Department of Biological Sciences, Fulbright College of Arts and Sciences, University of Arkansas, Fayetteville 72701.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.