Linked Life Data

1400448

Source:http://linkedlifedata.com/resource/pubmed/id/1400448

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
1992-11-25
pubmed:databankReference
pubmed:abstractText
Amino acid sequence information was obtained for the NH2 terminus, and for endogenous peptides generated by trypsin digestion, of a purified, truncated form of rat hepatic squalene synthase (RSS, EC 2.5.1.21) (Shechter, I., Klinger, E., Rucker, M. L., Engstrom, R. G., Spirito, J. A., Islam, M. A., Boettcher, B. R., and Weinstein, D. B. (1992) J. Biol. Chem. 267, 8628-8635). Degenerate primers, based on the amino acid sequences, were synthesized and used for the amplification and sequencing of a 1708-base pair (bp) cDNA for RSS from the rat hepatoma cell line H35. An open reading frame of 1248 bp encoding 416 amino acids (M(r) = 48,103) was detected for RSS. We have constructed a pRSS1327 expression vector by molecular cloning of a 1327-bp cDNA, which includes sequences of the entire coding region for RSS, into pBluescript. Expression in Escherichia coli of a functional, full-length RSS was confirmed by immunoblot analysis and enzymatic activity. We present and evaluate a model for the secondary structure of RSS and its possible membrane orientation. The model predicts a 315-residue domain at the center of the protein that contains the catalytic site and is released in a soluble form by partial proteolysis. The 33-residue NH2-terminal and 98-residue COOH-terminal sections are not involved in catalysis. Sequence analysis of the catalytic domain of RSS indicate three regions with high homology to sequences in a number of functionally distinct proteins that utilize polyprenyl diphosphate substrates.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
267
pubmed:geneSymbol
RSS
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21368-74
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Molecular cloning, expression, and characterization of the cDNA for the rat hepatic squalene synthase.
pubmed:affiliation
Eleanor Roosevelt Institute, Denver, Colorado 80206.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't