Linked Life Data

1281472

Source:http://linkedlifedata.com/resource/pubmed/id/1281472

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
1993-1-21
pubmed:databankReference
pubmed:abstractText
Glycogenin is a self-glucosylating protein involved in the initiation reactions of glycogen synthesis. Initiation occurs in two stages, requiring first the covalent attachment of a glucose residue to Tyr-194 of glycogenin and then elongation to form an oligosaccharide chain. The latter reaction is known to be catalyzed by glycogenin itself. The glycogenin sequence determined from the protein by Campbell and Cohen (Campbell, D. G., and Cohen, P. (1989) Eur. J. Biochem. 185, 119-125) was used to design oligonucleotide probes to screen a rabbit muscle lambda gt11 library. A cDNA was isolated that predicted an amino acid sequence identical to that of Campbell and Cohen, except that Cys residues replaced Ser-88 and Leu-97. Northern analysis indicated a strongly hybridizing message of 1.8 kilobases, present in most tissues including skeletal muscle, but much weaker in kidney and scarcely detectable in liver. A much weaker 3-kilobase message was also detected in muscle. Polymerase chain reaction was used to isolate DNA fragments encoding a portion of glycogenin from rat and cow. The sequence of this segment was > 90% identical at the amino acid level across the three species, indicating that glycogenin is a highly conserved protein. Using the pET-8c vector, the glycogenin protein was expressed in Escherichia coli. Incubation of the recombinant glycogenin with UDP-[14C]glucose and Mn2+ resulted in labeling of the glycogenin protein, indicating that the recombinant glycogenin was enzymatically active and capable of self-glucosylation. Furthermore, after incubation with UDP-glucose, the recombinant glycogenin could serve as a substrate for glycogen synthase, leading to the production of high M(r) polysaccharide. Therefore, production of functional glycogenin did not require the intervention of any other mammalian protein.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
25759-63
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:1281472-Amino Acid Sequence, pubmed-meshheading:1281472-Animals, pubmed-meshheading:1281472-Base Sequence, pubmed-meshheading:1281472-Blotting, Northern, pubmed-meshheading:1281472-Cloning, Molecular, pubmed-meshheading:1281472-Escherichia coli, pubmed-meshheading:1281472-Gene Library, pubmed-meshheading:1281472-Glucosyltransferases, pubmed-meshheading:1281472-Glycoproteins, pubmed-meshheading:1281472-Molecular Sequence Data, pubmed-meshheading:1281472-Molecular Weight, pubmed-meshheading:1281472-Muscle Proteins, pubmed-meshheading:1281472-Muscles, pubmed-meshheading:1281472-Oligonucleotide Probes, pubmed-meshheading:1281472-Polymerase Chain Reaction, pubmed-meshheading:1281472-RNA, pubmed-meshheading:1281472-Rabbits, pubmed-meshheading:1281472-Recombinant Proteins, pubmed-meshheading:1281472-Restriction Mapping, pubmed-meshheading:1281472-Sequence Homology, Amino Acid
pubmed:year
1992
pubmed:articleTitle
Rabbit skeletal muscle glycogenin. Molecular cloning and production of fully functional protein in Escherichia coli.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis 46202-5122.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't