Linked Life Data

7496400

Source:http://linkedlifedata.com/resource/pubmed/id/7496400

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1996-1-16
pubmed:databankReference
pubmed:abstractText
The enzyme 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR, EC 1.1.1.34) catalyses the synthesis of mevalonate, the committed precursor of the great variety of isoprenoid compounds and derivatives synthesized in higher plants. It has previously been reported that Arabidopsis thaliana contains two differentially expressed genes, HMG1 and HMG2, that encode two HMGR isoforms (HMGR1 and HMGR2, respectively). This paper reports the characterization of a novel HMGR mRNA (HMGR1L mRNA) derived from the HMG1 gene. This mRNA is initiated 121 bp upstream from the transcription start site previously characterized. In contrast with the previously reported HMGR1 mRNA (HMGR1S mRNA), which is detected at high levels in all tissues of the plant, HMGR1L mRNA is present at relatively low levels and its expression is restricted mostly to seedlings, roots and inflorescences. HMGR1L and HMGR1S mRNAs are transcribed from alternative promoters. HMGR1L mRNA contains an in-phase AUG start codon which allows the synthesis of a novel HMGR isoform (HMGR1L) having 50 additional amino acid residues at its N-terminal end. Using an in vitro transcription-translation system we have shown that HMGR1L is inserted into ER-derived microsomes. It is thus unlikely that the extended N-terminal region of HMGR1L might have a role in targeting the enzyme to plastids or mitochondria. These results support the previous proposal that the endoplasmic reticulum is the only cell compartment for the primary targeting of HMGR in Arabidopsis and reinforce the view that plant HMGR is under the control of complex mechanisms operating at both transcriptional and post-transcriptional levels.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0960-7412
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
541-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:7496400-Alternative Splicing, pubmed-meshheading:7496400-Amino Acid Sequence, pubmed-meshheading:7496400-Arabidopsis, pubmed-meshheading:7496400-Base Sequence, pubmed-meshheading:7496400-DNA Primers, pubmed-meshheading:7496400-Gene Expression Regulation, Enzymologic, pubmed-meshheading:7496400-Gene Expression Regulation, Plant, pubmed-meshheading:7496400-Genes, Plant, pubmed-meshheading:7496400-Hydroxymethylglutaryl CoA Reductases, pubmed-meshheading:7496400-Isoenzymes, pubmed-meshheading:7496400-Microsomes, pubmed-meshheading:7496400-Molecular Sequence Data, pubmed-meshheading:7496400-Organ Specificity, pubmed-meshheading:7496400-Polymerase Chain Reaction, pubmed-meshheading:7496400-Promoter Regions, Genetic, pubmed-meshheading:7496400-Protein Biosynthesis, pubmed-meshheading:7496400-RNA, Messenger, pubmed-meshheading:7496400-Recombinant Fusion Proteins, pubmed-meshheading:7496400-TATA Box, pubmed-meshheading:7496400-Transcription, Genetic
pubmed:year
1995
pubmed:articleTitle
The use of an alternative promoter in the Arabidopsis thaliana HMG1 gene generates an mRNA that encodes a novel 3-hydroxy-3-methylglutaryl coenzyme A reductase isoform with an extended N-terminal region.
pubmed:affiliation
Departament de Bioquímica i Biologia Molecular, Facultat de Química, Universitat de Barcelona, Spain.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't